The Full Wiki

Src (gene): Wikis

Advertisements
  

Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.

Encyclopedia

From Wikipedia, the free encyclopedia

edit
V-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian)

PDB rendering based on 1a07.
Available structures
1a07, 1a08, 1a09, 1a1a, 1a1b, 1a1c, 1a1e, 1bkl, 1bkm, 1f1w, 1f2f, 1fmk, 1hcs, 1hct, 1is0, 1kc2, 1ksw, 1nlo, 1nlp, 1nzl, 1nzv, 1o41, 1o42, 1o43, 1o44, 1o45, 1o46, 1o47, 1o48, 1o49, 1o4a, 1o4b, 1o4c, 1o4d, 1o4e, 1o4f, 1o4g, 1o4h, 1o4i, 1o4j, 1o4k, 1o4l, 1o4m, 1o4n, 1o4o, 1o4p, 1o4q, 1o4r, 1p13, 1prl, 1prm, 1qwe, 1qwf, 1rlp, 1rlq, 1sha, 1shb, 1shd, 1skj, 1spr, 1sps, 1srl, 1srm, 1y57, 1yi6, 1yoj, 1yol, 1yom, 2bdf, 2bdj, 2h8h, 2hwo, 2hwp, 2oiq, 2ptk, 2src
Identifiers
Symbols SRC; ASV; SRC1; c-SRC; p60-Src
External IDs OMIM190090 MGI98397 HomoloGene21120 GeneCards: SRC Gene
RNA expression pattern
PBB GE SRC 213324 at.png
PBB GE SRC 221284 s at.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6714 20779
Ensembl ENSG00000197122 ENSMUSG00000027646
UniProt P12931 Q2M4I4
RefSeq (mRNA) NM_005417 NM_001025395
RefSeq (protein) NP_005408 NP_001020566
Location (UCSC) Chr 20:
35.41 - 35.47 Mb
Chr 2:
157.12 - 157.16 Mb
PubMed search [1] [2]

Src (pronounced "sarc" as it is short for sarcoma) is a family of proto-oncogenic tyrosine kinases originally discovered by J. Michael Bishop and Harold E. Varmus, for which they won the 1989 Nobel Prize in Physiology or Medicine.[1] The discovery of Src family proteins has been instrumental to the modern understanding of cancer as a disease where normally healthy cellular signalling has gone awry.

This gene is similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene.[2]

Contents

v-src

Francis Peyton Rous first proposed that viruses can cause cancer. He proved it in 1911 and was later awarded the Nobel prize in 1966. Chickens grow a tumor called a fibrosarcoma. Rous ground up these sarcomas, centrifuged them to remove the solid material, and injected the remaining liquid into chicks. The chicks developed sarcomas. The causative agent in the liquid was a virus, now called Rous sarcoma virus (RSV).

Later work by others showed that RSV was a type of retrovirus. Non-cancer-forming retroviruses contain three genes, called gag, pol, and env. Some tumor-inducing retroviruses (such as RSV), however, also contain a gene called v-src (viral-sarcoma). It was found that the v-src gene in RSV is required for the formation of cancer and that the other genes have no role in oncogenesis.[3]

A function for Src tyrosine kinases in normal cell growth was first demonstrated with the binding of family member p56lck to the cytoplasmic tail of the CD4 and CD8 co-receptors on T-cells.[4] Src tyrosine kinases also transmit integrin-dependent signals central to cell movement and proliferation. Hallmarks of v-src induced transformation are rounding of the cell and the formation of actin rich podosomes on the basal surface of the cell. These structures are correlated with increased invasiveness, a process thought to be essential for metastasis.

v-src lacks the C-terminal inhibitory phosphorylation site (tyrosine-527), and is therefore constitutively active as opposed to normal src (c-src) which is only activated under certain circumstances where it is required (e.g. growth factor signaling). v-src is therefore an instructive example of an oncogene whereas c-src is a proto-oncogene.

c-src

In 1979, J. Michael Bishop and Harold E. Varmus discovered that normal chickens contain a gene that is structurally closely-related to v-src.[3] The normal cellular gene was called c-src (cellular-src).[5] This discovery changed the current thinking about cancer from a model wherein cancer is caused by a foreign substance (a viral gene) to one where a gene that is normally present in the cell can cause cancer. It is believed that at one point an ancestral virus mistakenly incorporated the c-src gene of its cellular host. At some point, the normal gene became mutated into an abnormally-functioning oncogene, as is now observed in RSV. Once the oncogene is transfected back into a normal host, it can lead to cancer.

src: The transforming (sarcoma inducing) gene of Rous sarcoma virus. The protein product is pp60vsrc, a cytoplasmic protein with tyrosine-specific protein kinase activity (EC 2.7.10.2), that associates with the cytoplasmic face of the plasma membrane. The protein consists of three domains, an N-terminal SH3 domain, a central SH2 domain and a tyrosine kinase domain. The SH2 and SH3 domains cooperate in the auto-inhibition of the kinase domain. c-Src is phosphorylated on an inhibitory tyrosine near the c-terminus of the protein. This produces a binding site for the SH2 domain which, when bound, facilitates binding of the SH3 domain to a low affinity polyproline site within the linker between the SH2 domain and the kinase domain. Binding of the SH3 domain results in misalignment of residues within the kinase domain's active site inactivating the enzyme. This allows for multiple mechanism for c-Src activation: dephosphorylation of the C-terminal tyrosine by a protein tyrosine phosphatase, binding of the SH2 domain by a competitive phospho-tyrosine residue, as seen in the case of c-Src binding to focal adhesion kinase, or competitive binding of a polyproline binding site to the SH3 domain, as seen in the case of the HIV NEF protein.

Src family kinases

The Src family includes nine mammalian members: Src, Yes, Fyn, and Fgr, forming the SrcA subfamily, Lck, Hck, Blk, and Lyn in the SrcB subfamily, and Frk in its own subfamily. Frk has homologs in invertebrates such as flies and worms, and Src homologs exist in organisms as diverse as unicellular choanoflagellates, but the SrcA and SrcB subfamilies are specific to vertebrates.

Src family kinases interact with a lot of cellular cytosolic, nuclear and membrane proteins and modify these proteins by phosphorylation on tyrosine residues. With the advent a number of substrates have been discovered.[6]

Interactions

Src (gene) has been shown to interact with GRIN2A,[7][8] C-Raf,[9] CD44,[10] Aryl hydrocarbon receptor nuclear translocator,[11] Aryl hydrocarbon receptor,[11] PDE6G,[12] STAT1,[13][14] EPH receptor B2,[15][16] Androgen receptor,[17][18][19] Protein kinase Mζ,[20] STAT3,[21] Grb2,[12][22] Beta-3 adrenergic receptor,[23] Beta adrenergic receptor kinase,[12] Epidermal growth factor receptor,[13][24][25] PTK2,[26][27][28][29][30][31] DAB2,[32] EPS8,[33] Dystroglycan,[34] Estrogen receptor alpha,[17][35][36][37] Estrogen receptor beta,[17][37] HNF1A,[38] KHDRBS1,[39][40][41][42][43] DDEF1,[44] MUC1,[45][46] PTK2B,[24][47][48] BCAR1,[49][50][26][51][52][28] SHB,[53] PLD2,[54] Serum response factor,[55] NCOA6,[56][57][58][59] Retinoic acid receptor alpha,[36][60] Wiskott-Aldrich syndrome protein,[61][62] RICS,[63] RAS p21 protein activator 1,[64][65] MT-ND2[66] and GNB2L1.[67]

Overview of signal transduction pathways involved in apoptosis.

See also

External links

References

  1. ^ Nobel Prize in Physiology or Medicine for 1989 jointly to J. Michael Bishop and Harold E. Varmus for their discovery of "the cellular origin of retroviral oncogenes". Press Release.
  2. ^ "Entrez Gene: SRC v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6714.  
  3. ^ a b Stehelin D, Fujita DJ, Padgett T, Varmus HE, Bishop JM. (1977). "Detection and enumeration of transformation-defective strains of avian sarcoma virus with molecular hybridization". Virology 76 (2): 675–84. doi:10.1016/0042-6822(77)90250-1. PMID 190771.  
  4. ^ Rudd CE, Trevillyan JM, Dasgupta JD, Wong LL, Schlossman SF (July 1988). "The CD4 receptor is complexed in detergent lysates to a protein-tyrosine kinase (pp58) from human T lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 85 (14): 5190–4. doi:10.1073/pnas.85.14.5190. PMID 2455897. PMC 281714. http://www.pnas.org/content/85/14/5190.abstract.  
  5. ^ Oppermann H, Levinson AD, Varmus HE, Levintow L, Bishop JM (1979). "Uninfected vertebrate cells contain a protein that is closely related to the product of the avian sarcoma virus transforming gene (src)". Proc Natl Acad Sci U S A. 76 (4): 1804–8. doi:10.1073/pnas.76.4.1804. PMID 221907.  
  6. ^ Amanchy R, Zhong J, Hong R, Kim JH, Gucek M, Molina H, Pandey A. Identification of c-Src tyrosine kinase substrates in PDGF receptor signaling pathway. Molecular Oncology DOI: 10.1016/j.molonc.2009.07.001 Amanchy R, Iwahori A, Molina H, Kalume DE, Gronborg M, Joore J, Cope L, Pandey A. Identification of c-Src tyrosine kinase substrates using mass spectrometry and peptide microarrays Journal of Proteome Research. 2008 Sep;7(9):3900-10. Luo W, Slebos RJ, Hill S, Li M, Brábek J, Amanchy R, Chaerkady R, Pandey A, Ham AL and Hanks SK. Global impact of oncogenic Src on a phosphotyrosine proteome Journal of Proteome Research. 2008 Aug;7(8):3447-60.
  7. ^ Ma, Juan; Zhang Guang-Yi (Sep. 2003). "Lithium reduced N-methyl-D-aspartate receptor subunit 2A tyrosine phosphorylation and its interactions with Src and Fyn mediated by PSD-95 in rat hippocampus following cerebral ischemia". Neurosci. Lett. (Ireland) 348 (3): 185–9. ISSN 0304-3940. PMID 12932824.  
  8. ^ Takagi, N; Cheung H H, Bissoon N, Teves L, Wallace M C, Gurd J W (Aug. 1999). "The effect of transient global ischemia on the interaction of Src and Fyn with the N-methyl-D-aspartate receptor and postsynaptic densities: possible involvement of Src homology 2 domains". J. Cereb. Blood Flow Metab. (UNITED STATES) 19 (8): 880–8. doi:10.1097/00004647-199908000-00007. ISSN 0271-678X. PMID 10458595.  
  9. ^ Cleghon, V; Morrison D K (Jul. 1994). "Raf-1 interacts with Fyn and Src in a non-phosphotyrosine-dependent manner". J. Biol. Chem. (UNITED STATES) 269 (26): 17749–55. ISSN 0021-9258. PMID 7517401.  
  10. ^ Bourguignon, L Y; Zhu H, Shao L, Chen Y W (Mar. 2001). "CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic acid-dependent ovarian tumor cell migration". J. Biol. Chem. (United States) 276 (10): 7327–36. doi:10.1074/jbc.M006498200. ISSN 0021-9258. PMID 11084024.  
  11. ^ a b Beischlag, Timothy V; Wang Song, Rose David W, Torchia Joseph, Reisz-Porszasz Suzanne, Muhammad Khurshid, Nelson Walter E, Probst Markus R, Rosenfeld Michael G, Hankinson Oliver (Jun. 2002). "Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex". Mol. Cell. Biol. (United States) 22 (12): 4319–33. ISSN 0270-7306. PMID 12024042.  
  12. ^ a b c Wan, Kah Fei; Sambi Balwinder S, Tate Rothwelle, Waters Catherine, Pyne Nigel J (May. 2003). "The inhibitory gamma subunit of the type 6 retinal cGMP phosphodiesterase functions to link c-Src and G-protein-coupled receptor kinase 2 in a signaling unit that regulates p42/p44 mitogen-activated protein kinase by epidermal growth factor". J. Biol. Chem. (United States) 278 (20): 18658–63. doi:10.1074/jbc.M212103200. ISSN 0021-9258. PMID 12624098.  
  13. ^ a b Olayioye, M A; Beuvink I, Horsch K, Daly J M, Hynes N E (Jun. 1999). "ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases". J. Biol. Chem. (UNITED STATES) 274 (24): 17209–18. ISSN 0021-9258. PMID 10358079.  
  14. ^ Cirri, P; Chiarugi P, Marra F, Raugei G, Camici G, Manao G, Ramponi G (Oct. 1997). "c-Src activates both STAT1 and STAT3 in PDGF-stimulated NIH3T3 cells". Biochem. Biophys. Res. Commun. (UNITED STATES) 239 (2): 493–7. doi:10.1006/bbrc.1997.7493. ISSN 0006-291X. PMID 9344858.  
  15. ^ Zisch, A H; Kalo M S, Chong L D, Pasquale E B (May. 1998). "Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region". Oncogene (ENGLAND) 16 (20): 2657–70. doi:10.1038/sj.onc.1201823. ISSN 0950-9232. PMID 9632142.  
  16. ^ Zisch, A H; Pazzagli C, Freeman A L, Schneller M, Hadman M, Smith J W, Ruoslahti E, Pasquale E B (Jan. 2000). "Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses". Oncogene (ENGLAND) 19 (2): 177–87. doi:10.1038/sj.onc.1203304. ISSN 0950-9232. PMID 10644995.  
  17. ^ a b c Migliaccio, A; Castoria G, Di Domenico M, de Falco A, Bilancio A, Lombardi M, Barone M V, Ametrano D, Zannini M S, Abbondanza C, Auricchio F (Oct. 2000). "Steroid-induced androgen receptor-oestradiol receptor beta-Src complex triggers prostate cancer cell proliferation". EMBO J. (ENGLAND) 19 (20): 5406–17. doi:10.1093/emboj/19.20.5406. ISSN 0261-4189. PMID 11032808.  
  18. ^ Unni, Emmanual; Sun Shihua, Nan Bicheng, McPhaul Michael J, Cheskis Boris, Mancini Michael A, Marcelli Marco (Oct. 2004). "Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence". Cancer Res. (United States) 64 (19): 7156–68. doi:10.1158/0008-5472.CAN-04-1121. ISSN 0008-5472. PMID 15466214.  
  19. ^ Powell, S M; Christiaens V, Voulgaraki D, Waxman J, Claessens F, Bevan C L (Mar. 2004). "Mechanisms of androgen receptor signalling via steroid receptor coactivator-1 in prostate". Endocr. Relat. Cancer (England) 11 (1): 117–30. ISSN 1351-0088. PMID 15027889.  
  20. ^ Seibenhener, M L; Roehm J, White W O, Neidigh K B, Vandenplas M L, Wooten M W (Jul. 1999). "Identification of Src as a novel atypical protein kinase C-interacting protein". Mol. Cell Biol. Res. Commun. (UNITED STATES) 2 (1): 28–31. doi:10.1006/mcbr.1999.0140. ISSN 1522-4724. PMID 10527887.  
  21. ^ Cao, X; Tay A, Guy G R, Tan Y H (Apr. 1996). "Activation and association of Stat3 with Src in v-Src-transformed cell lines". Mol. Cell. Biol. (UNITED STATES) 16 (4): 1595–603. ISSN 0270-7306. PMID 8657134.  
  22. ^ Saci, Abdelhafid; Liu Wang-Qing, Vidal Michel, Garbay Christiane, Rendu Francine, Bachelot-Loza Christilla (May. 2002). "Differential effect of the inhibition of Grb2-SH3 interactions in platelet activation induced by thrombin and by Fc receptor engagement". Biochem. J. (England) 363 (Pt 3): 717–25. ISSN 0264-6021. PMID 11964172.  
  23. ^ Cao, W; Luttrell L M, Medvedev A V, Pierce K L, Daniel K W, Dixon T M, Lefkowitz R J, Collins S (Dec. 2000). "Direct binding of activated c-Src to the beta 3-adrenergic receptor is required for MAP kinase activation". J. Biol. Chem. (UNITED STATES) 275 (49): 38131–4. doi:10.1074/jbc.C000592200. ISSN 0021-9258. PMID 11013230.  
  24. ^ a b Keely, S J; Calandrella S O, Barrett K E (Apr. 2000). "Carbachol-stimulated transactivation of epidermal growth factor receptor and mitogen-activated protein kinase in T(84) cells is mediated by intracellular ca(2+), PYK-2, and p60(src)". J. Biol. Chem. (UNITED STATES) 275 (17): 12619–25. ISSN 0021-9258. PMID 10777553.  
  25. ^ Sato, K; Kimoto M, Kakumoto M, Horiuchi D, Iwasaki T, Tokmakov A A, Fukami Y (Sep. 2000). "Adaptor protein Shc undergoes translocation and mediates up-regulation of the tyrosine kinase c-Src in EGF-stimulated A431 cells". Genes Cells (ENGLAND) 5 (9): 749–64. ISSN 1356-9597. PMID 10971656.  
  26. ^ a b Hsia, Datsun A; Mitra Satyajit K, Hauck Christof R, Streblow Daniel N, Nelson Jay A, Ilic Dusko, Huang Shuang, Li Erguang, Nemerow Glen R, Leng Jay, Spencer Kathryn S R, Cheresh David A, Schlaepfer David D (Mar. 2003). "Differential regulation of cell motility and invasion by FAK". J. Cell Biol. (United States) 160 (5): 753–67. doi:10.1083/jcb.200212114. ISSN 0021-9525. PMID 12615911.  
  27. ^ Hecker, Timothy P; Grammer J Robert, Gillespie G Yancey, Stewart Jerry, Gladson Candece L (May. 2002). "Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples". Cancer Res. (United States) 62 (9): 2699–707. ISSN 0008-5472. PMID 11980671.  
  28. ^ a b Angers-Loustau, A; Côté J F, Charest A, Dowbenko D, Spencer S, Lasky L A, Tremblay M L (Mar. 1999). "Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts". J. Cell Biol. (UNITED STATES) 144 (5): 1019–31. ISSN 0021-9525. PMID 10085298.  
  29. ^ Relou, Ingrid A M; Bax Liane A B, van Rijn Herman J M, Akkerman Jan-Willem N (Jan. 2003). "Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein". Biochem. J. (England) 369 (Pt 2): 407–16. doi:10.1042/BJ20020410. ISSN 0264-6021. PMID 12387730.  
  30. ^ Messina, Samantha; Onofri Franco, Bongiorno-Borbone Lucilla, Giovedì Silvia, Valtorta Flavia, Girault Jean-Antoine, Benfenati Fabio (Jan. 2003). "Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin". J. Neurochem. (England) 84 (2): 253–65. ISSN 0022-3042. PMID 12558988.  
  31. ^ Lebrun, P; Mothe-Satney I, Delahaye L, Van Obberghen E, Baron V (Nov. 1998). "Insulin receptor substrate-1 as a signaling molecule for focal adhesion kinase pp125(FAK) and pp60(src)". J. Biol. Chem. (UNITED STATES) 273 (48): 32244–53. ISSN 0021-9258. PMID 9822703.  
  32. ^ Zhou, Jian; Scholes Jessica, Hsieh Jer-Tsong (Feb. 2003). "Characterization of a novel negative regulator (DOC-2/DAB2) of c-Src in normal prostatic epithelium and cancer". J. Biol. Chem. (United States) 278 (9): 6936–41. doi:10.1074/jbc.M210628200. ISSN 0021-9258. PMID 12473651.  
  33. ^ Maa, M C; Lai J R, Lin R W, Leu T H (Jul. 1999). "Enhancement of tyrosyl phosphorylation and protein expression of eps8 by v-Src". Biochim. Biophys. Acta (NETHERLANDS) 1450 (3): 341–51. ISSN 0006-3002. PMID 10395945.  
  34. ^ Sotgia, F; Lee H, Bedford M T, Petrucci T, Sudol M, Lisanti M P (Dec. 2001). "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins". Biochemistry (United States) 40 (48): 14585–92. ISSN 0006-2960. PMID 11724572.  
  35. ^ Teo, A K; Oh H K, Ali R B, Li B F (Oct. 2001). "The modified human DNA repair enzyme O(6)-methylguanine-DNA methyltransferase is a negative regulator of estrogen receptor-mediated transcription upon alkylation DNA damage". Mol. Cell. Biol. (United States) 21 (20): 7105–14. doi:10.1128/MCB.21.20.7105-7114.2001. ISSN 0270-7306. PMID 11564893.  
  36. ^ a b Kim, H J; Yi J Y, Sung H S, Moore D D, Jhun B H, Lee Y C, Lee J W (Sep. 1999). "Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation". Mol. Cell. Biol. (UNITED STATES) 19 (9): 6323–32. ISSN 0270-7306. PMID 10454579.  
  37. ^ a b Slentz-Kesler, K; Moore J T, Lombard M, Zhang J, Hollingsworth R, Weiner M P (Oct. 2000). "Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor beta". Genomics (UNITED STATES) 69 (1): 63–71. doi:10.1006/geno.2000.6299. ISSN 0888-7543. PMID 11013076.  
  38. ^ Soutoglou, E; Papafotiou G, Katrakili N, Talianidis I (Apr. 2000). "Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins". J. Biol. Chem. (UNITED STATES) 275 (17): 12515–20. ISSN 0021-9258. PMID 10777539.  
  39. ^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (Sep. 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16179252.  
  40. ^ Oneyama, Chitose; Nakano Hirofumi, Sharma Sreenath V (Mar. 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug". Oncogene (England) 21 (13): 2037–50. doi:10.1038/sj.onc.1205271. ISSN 0950-9232. PMID 11960376.  
  41. ^ Koch, C A; Moran M F, Anderson D, Liu X Q, Mbamalu G, Pawson T (Mar. 1992). "Multiple SH2-mediated interactions in v-src-transformed cells". Mol. Cell. Biol. (UNITED STATES) 12 (3): 1366–74. ISSN 0270-7306. PMID 1545818.  
  42. ^ Shen, Z; Batzer A, Koehler J A, Polakis P, Schlessinger J, Lydon N B, Moran M F (Aug. 1999). "Evidence for SH3 domain directed binding and phosphorylation of Sam68 by Src". Oncogene (ENGLAND) 18 (33): 4647–53. doi:10.1038/sj.onc.1203079. ISSN 0950-9232. PMID 10467411.  
  43. ^ Finan, P M; Hall A, Kellie S (Jul. 1996). "Sam68 from an immortalised B-cell line associates with a subset of SH3 domains". FEBS Lett. (NETHERLANDS) 389 (2): 141–4. ISSN 0014-5793. PMID 8766817.  
  44. ^ Brown, M T; Andrade J, Radhakrishna H, Donaldson J G, Cooper J A, Randazzo P A (Dec. 1998). "ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src". Mol. Cell. Biol. (UNITED STATES) 18 (12): 7038–51. ISSN 0270-7306. PMID 9819391.  
  45. ^ Li, Y; Kuwahara H, Ren J, Wen G, Kufe D (Mar. 2001). "The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin". J. Biol. Chem. (United States) 276 (9): 6061–4. doi:10.1074/jbc.C000754200. ISSN 0021-9258. PMID 11152665.  
  46. ^ Li, Y; Ren J, Yu W, Li Q, Kuwahara H, Yin L, Carraway K L, Kufe D (Sep. 2001). "The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin". J. Biol. Chem. (United States) 276 (38): 35239–42. doi:10.1074/jbc.C100359200. ISSN 0021-9258. PMID 11483589.  
  47. ^ Kumar, S; Avraham S, Bharti A, Goyal J, Pandey P, Kharbanda S (Oct. 1999). "Negative regulation of PYK2/related adhesion focal tyrosine kinase signal transduction by hematopoietic tyrosine phosphatase SHPTP1". J. Biol. Chem. (UNITED STATES) 274 (43): 30657–63. ISSN 0021-9258. PMID 10521452.  
  48. ^ Dikic, I; Tokiwa G, Lev S, Courtneidge S A, Schlessinger J (Oct. 1996). "A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation". Nature (ENGLAND) 383 (6600): 547–50. doi:10.1038/383547a0. ISSN 0028-0836. PMID 8849729.  
  49. ^ Burnham, M R; Harte M T, Bouton A H (Sep. 1999). "The role of SRC-CAS interactions in cellular transformation: ectopic expression of the carboxy terminus of CAS inhibits SRC-CAS interaction but has no effect on cellular transformation". Mol. Carcinog. (UNITED STATES) 26 (1): 20–31. ISSN 0899-1987. PMID 10487518.  
  50. ^ Wei, Lin; Yang Yu, Zhang Xin, Yu Qiang (2002). "Anchorage-independent phosphorylation of p130(Cas) protects lung adenocarcinoma cells from anoikis". J. Cell. Biochem. (United States) 87 (4): 439–49. doi:10.1002/jcb.10322. ISSN 0730-2312. PMID 12397603.  
  51. ^ Kovacic-Milivojević, B; Roediger F, Almeida E A, Damsky C H, Gardner D G, Ilić D (Aug. 2001). "Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophy". Mol. Biol. Cell (United States) 12 (8): 2290–307. ISSN 1059-1524. PMID 11514617.  
  52. ^ Donaldson, J C; Dempsey P J, Reddy S, Bouton A H, Coffey R J, Hanks S K (Apr. 2000). "Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells". Exp. Cell Res. (UNITED STATES) 256 (1): 168–78. doi:10.1006/excr.2000.4822. ISSN 0014-4827. PMID 10739664.  
  53. ^ Karlsson, T; Songyang Z, Landgren E, Lavergne C, Di Fiore P P, Anafi M, Pawson T, Cantley L C, Claesson-Welsh L, Welsh M (Apr. 1995). "Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins". Oncogene (ENGLAND) 10 (8): 1475–83. ISSN 0950-9232. PMID 7537362.  
  54. ^ Ahn, Bong-Hyun; Kim Shi Yeon, Kim Eun Hee, Choi Kyeong Sook, Kwon Taeg Kyu, Lee Young Han, Chang Jong-Soo, Kim Myung-Suk, Jo Yang-Hyeok, Min Do Sik (May. 2003). "Transmodulation between phospholipase D and c-Src enhances cell proliferation". Mol. Cell. Biol. (United States) 23 (9): 3103–15. ISSN 0270-7306. PMID 12697812.  
  55. ^ Kim, H J; Kim J H, Lee J W (Oct. 1998). "Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations". J. Biol. Chem. (UNITED STATES) 273 (44): 28564–7. ISSN 0021-9258. PMID 9786846.  
  56. ^ Goo, Young-Hwa; Sohn Young Chang, Kim Dae-Hwan, Kim Seung-Whan, Kang Min-Jung, Jung Dong-Ju, Kwak Eunyee, Barlev Nickolai A, Berger Shelley L, Chow Vincent T, Roeder Robert G, Azorsa David O, Meltzer Paul S, Suh Pan-Gil, Song Eun Joo, Lee Kong-Joo, Lee Young Chul, Lee Jae Woon (Jan. 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. (United States) 23 (1): 140–9. ISSN 0270-7306. PMID 12482968.  
  57. ^ Lee, S K; Anzick S L, Choi J E, Bubendorf L, Guan X Y, Jung Y K, Kallioniemi O P, Kononen J, Trent J M, Azorsa D, Jhun B H, Cheong J H, Lee Y C, Meltzer P S, Lee J W (Nov. 1999). "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". J. Biol. Chem. (UNITED STATES) 274 (48): 34283–93. ISSN 0021-9258. PMID 10567404.  
  58. ^ Lee, S K; Na S Y, Jung S Y, Choi J E, Jhun B H, Cheong J, Meltzer P S, Lee Y C, Lee J W (Jun. 2000). "Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2". Mol. Endocrinol. (UNITED STATES) 14 (6): 915–25. ISSN 0888-8809. PMID 10847592.  
  59. ^ Lee, S K; Jung S Y, Kim Y S, Na S Y, Lee Y C, Lee J W (Feb. 2001). "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. (United States) 15 (2): 241–54. ISSN 0888-8809. PMID 11158331.  
  60. ^ He, Bin; Wilson Elizabeth M (Mar. 2003). "Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs". Mol. Cell. Biol. (United States) 23 (6): 2135–50. ISSN 0270-7306. PMID 12612084.  
  61. ^ Banin, S; Truong O, Katz D R, Waterfield M D, Brickell P M, Gout I (Aug. 1996). "Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases". Curr. Biol. (ENGLAND) 6 (8): 981–8. ISSN 0960-9822. PMID 8805332.  
  62. ^ Finan, P M; Soames C J, Wilson L, Nelson D L, Stewart D M, Truong O, Hsuan J J, Kellie S (Oct. 1996). "Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains". J. Biol. Chem. (UNITED STATES) 271 (42): 26291–5. ISSN 0021-9258. PMID 8824280.  
  63. ^ Moon, Sun Young; Zang Heesuk, Zheng Yi (Feb. 2003). "Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP". J. Biol. Chem. (United States) 278 (6): 4151–9. doi:10.1074/jbc.M207789200. ISSN 0021-9258. PMID 12454018.  
  64. ^ Brott, B K; Decker S, O'Brien M C, Jove R (Oct. 1991). "Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein". Mol. Cell. Biol. (UNITED STATES) 11 (10): 5059–67. ISSN 0270-7306. PMID 1717825.  
  65. ^ Giglione, C; Gonfloni S, Parmeggiani A (Jun. 2001). "Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm". Eur. J. Biochem. (Germany) 268 (11): 3275–83. ISSN 0014-2956. PMID 11389730.  
  66. ^ Gingrich, Jeffrey R; Pelkey Kenneth A, Fam Sami R, Huang Yueqiao, Petralia Ronald S, Wenthold Robert J, Salter Michael W (Apr. 2004). "Unique domain anchoring of Src to synaptic NMDA receptors via the mitochondrial protein NADH dehydrogenase subunit 2". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (16): 6237–42. doi:10.1073/pnas.0401413101. ISSN 0027-8424. PMID 15069201.  
  67. ^ Chang, B Y; Conroy K B, Machleder E M, Cartwright C A (Jun. 1998). "RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells". Mol. Cell. Biol. (UNITED STATES) 18 (6): 3245–56. ISSN 0270-7306. PMID 9584165.  
  • Lodish, Harvey; Burk, Arnold; Zipurksy, Lawrence, et al. "Cancer" in Molecular Cell Biology. 4th edition. 2000. ISBN 0-7167-3706-X. [3]

Further reading

Advertisements

Advertisements






Got something to say? Make a comment.
Your name
Your email address
Message