Abstract
Csk phosphorylates Src family members at a key regulatory tyrosine in the C-terminal tail and suppresses their activities. It is not known whether Csk activity is regulated. To examine the features of Csk required for Src suppression, we expressed Csk mutants in a cell line with a disrupted csk gene. Expression of wild-type Csk suppressed Src, but Csk with mutations in the SH2, SH3, and catalytic domains did not suppress Src. An SH3 deletion mutant of Csk was fully active against in vitro substrates, but two SH2 domain mutants were essentially inactive. Whereas Src repressed by Csk was predominantly perinuclear, the activated Src in cells lacking Csk was localized to structures resembling podosomes. Activated mutant Src was also in podosomes, even in the presence of Csk. When Src was not active, Csk was diffusely located in the cytosol, but when Src was active, Csk colocalized with activated Src to podosomes. Csk also localizes to podosomes of cells transformed by an activated Src that lacks the major tyrosine autophosphorylation site, suggesting that the relocalization of Csk is not a consequence of the binding of the Csk SH2 domain to phosphorylated Src. A catalytically inactive Csk mutant also localized with Src to podosomes, but SH3 and SH2 domain mutants did not, suggesting that the SH3 and SH2 domains are both necessary to target Csk to places where Src is active. The failure of the catalytically active SH3 mutant of Csk to regulate Src may be due to its inability to colocalize with active Src.
Full text
PDF









Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bagrodia S., Taylor S. J., Shalloway D. Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis. Mol Cell Biol. 1993 Mar;13(3):1464–1470. doi: 10.1128/mcb.13.3.1464. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bar-Sagi D., Rotin D., Batzer A., Mandiyan V., Schlessinger J. SH3 domains direct cellular localization of signaling molecules. Cell. 1993 Jul 16;74(1):83–91. doi: 10.1016/0092-8674(93)90296-3. [DOI] [PubMed] [Google Scholar]
- Bennett B. D., Cowley S., Jiang S., London R., Deng B., Grabarek J., Groopman J. E., Goeddel D. V., Avraham H. Identification and characterization of a novel tyrosine kinase from megakaryocytes. J Biol Chem. 1994 Jan 14;269(2):1068–1074. [PubMed] [Google Scholar]
- Bergman M., Mustelin T., Oetken C., Partanen J., Flint N. A., Amrein K. E., Autero M., Burn P., Alitalo K. The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 1992 Aug;11(8):2919–2924. doi: 10.1002/j.1460-2075.1992.tb05361.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burridge K., Fath K. Focal contacts: transmembrane links between the extracellular matrix and the cytoskeleton. Bioessays. 1989 Apr;10(4):104–108. doi: 10.1002/bies.950100403. [DOI] [PubMed] [Google Scholar]
- Burridge K., Fath K., Kelly T., Nuckolls G., Turner C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol. 1988;4:487–525. doi: 10.1146/annurev.cb.04.110188.002415. [DOI] [PubMed] [Google Scholar]
- Cantley L. C., Auger K. R., Carpenter C., Duckworth B., Graziani A., Kapeller R., Soltoff S. Oncogenes and signal transduction. Cell. 1991 Jan 25;64(2):281–302. doi: 10.1016/0092-8674(91)90639-g. [DOI] [PubMed] [Google Scholar]
- Cartwright C. A., Eckhart W., Simon S., Kaplan P. L. Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain. Cell. 1987 Apr 10;49(1):83–91. doi: 10.1016/0092-8674(87)90758-6. [DOI] [PubMed] [Google Scholar]
- Chow L. M., Fournel M., Davidson D., Veillette A. Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk. Nature. 1993 Sep 9;365(6442):156–160. doi: 10.1038/365156a0. [DOI] [PubMed] [Google Scholar]
- Clark E. A., Brugge J. S. Redistribution of activated pp60c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets. Mol Cell Biol. 1993 Mar;13(3):1863–1871. doi: 10.1128/mcb.13.3.1863. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cobb B. S., Schaller M. D., Leu T. H., Parsons J. T. Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK. Mol Cell Biol. 1994 Jan;14(1):147–155. doi: 10.1128/mcb.14.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cooper J. A., Howell B. The when and how of Src regulation. Cell. 1993 Jun 18;73(6):1051–1054. doi: 10.1016/0092-8674(93)90634-3. [DOI] [PubMed] [Google Scholar]
- Cooper J. A., King C. S. Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src. Mol Cell Biol. 1986 Dec;6(12):4467–4477. doi: 10.1128/mcb.6.12.4467. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cooper J. A., MacAuley A. Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4232–4236. doi: 10.1073/pnas.85.12.4232. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cross F. R., Garber E. A., Pellman D., Hanafusa H. A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol Cell Biol. 1984 Sep;4(9):1834–1842. doi: 10.1128/mcb.4.9.1834. [DOI] [PMC free article] [PubMed] [Google Scholar]
- David-Pfeuty T., Nouvian-Dooghe Y. Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells. J Cell Biol. 1990 Dec;111(6 Pt 2):3097–3116. doi: 10.1083/jcb.111.6.3097. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DeClue J. E., Sadowski I., Martin G. S., Pawson T. A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9064–9068. doi: 10.1073/pnas.84.24.9064. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Devary Y., Gottlieb R. A., Smeal T., Karin M. The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases. Cell. 1992 Dec 24;71(7):1081–1091. doi: 10.1016/s0092-8674(05)80058-3. [DOI] [PubMed] [Google Scholar]
- Flynn D. C., Leu T. H., Reynolds A. B., Parsons J. T. Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate. Mol Cell Biol. 1993 Dec;13(12):7892–7900. doi: 10.1128/mcb.13.12.7892. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fukui Y., O'Brien M. C., Hanafusa H. Deletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrix. Mol Cell Biol. 1991 Mar;11(3):1207–1213. doi: 10.1128/mcb.11.3.1207. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gout I., Dhand R., Hiles I. D., Fry M. J., Panayotou G., Das P., Truong O., Totty N. F., Hsuan J., Booker G. W. The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell. 1993 Oct 8;75(1):25–36. [PubMed] [Google Scholar]
- Hirai H., Varmus H. E. Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8592–8596. doi: 10.1073/pnas.87.21.8592. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Iba H., Cross F. R., Garber E. A., Hanafusa H. Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src. Mol Cell Biol. 1985 May;5(5):1058–1066. doi: 10.1128/mcb.5.5.1058. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Imamoto A., Soriano P. Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice. Cell. 1993 Jun 18;73(6):1117–1124. doi: 10.1016/0092-8674(93)90641-3. [DOI] [PubMed] [Google Scholar]
- Jove R., Hanafusa H. Cell transformation by the viral src oncogene. Annu Rev Cell Biol. 1987;3:31–56. doi: 10.1146/annurev.cb.03.110187.000335. [DOI] [PubMed] [Google Scholar]
- Kamps M. P., Buss J. E., Sefton B. M. Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation. Cell. 1986 Apr 11;45(1):105–112. doi: 10.1016/0092-8674(86)90542-8. [DOI] [PubMed] [Google Scholar]
- Kamps M. P., Sefton B. M. Most of the substrates of oncogenic viral tyrosine protein kinases can be phosphorylated by cellular tyrosine protein kinases in normal cells. Oncogene Res. 1988 Sep;3(2):105–115. [PubMed] [Google Scholar]
- Kanner S. B., Reynolds A. B., Wang H. C., Vines R. R., Parsons J. T. The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110. EMBO J. 1991 Jul;10(7):1689–1698. doi: 10.1002/j.1460-2075.1991.tb07693.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kaplan J. M., Varmus H. E., Bishop J. M. The src protein contains multiple domains for specific attachment to membranes. Mol Cell Biol. 1990 Mar;10(3):1000–1009. doi: 10.1128/mcb.10.3.1000. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kaplan K. B., Swedlow J. R., Varmus H. E., Morgan D. O. Association of p60c-src with endosomal membranes in mammalian fibroblasts. J Cell Biol. 1992 Jul;118(2):321–333. doi: 10.1083/jcb.118.2.321. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Klages S., Adam D., Class K., Fargnoli J., Bolen J. B., Penhallow R. C. Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme family. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2597–2601. doi: 10.1073/pnas.91.7.2597. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kmiecik T. E., Shalloway D. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell. 1987 Apr 10;49(1):65–73. doi: 10.1016/0092-8674(87)90756-2. [DOI] [PubMed] [Google Scholar]
- Koch C. A., Anderson D., Moran M. F., Ellis C., Pawson T. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science. 1991 May 3;252(5006):668–674. doi: 10.1126/science.1708916. [DOI] [PubMed] [Google Scholar]
- Krueger J. G., Garber E. A., Chin S. S., Hanafusa H., Goldberg A. R. Size-variant pp60src proteins of recovered avian sarcoma viruses interact with adhesion plaques as peripheral membrane proteins: effects on cell transformation. Mol Cell Biol. 1984 Mar;4(3):454–467. doi: 10.1128/mcb.4.3.454. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krueger J. G., Garber E. A., Goldberg A. R. Subcellular localization of pp60src in RSV-transformed cells. Curr Top Microbiol Immunol. 1983;107:51–124. [PubMed] [Google Scholar]
- Kypta R. M., Goldberg Y., Ulug E. T., Courtneidge S. A. Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell. 1990 Aug 10;62(3):481–492. doi: 10.1016/0092-8674(90)90013-5. [DOI] [PubMed] [Google Scholar]
- Liebl E. C., Martin G. S. Intracellular targeting of pp60src expression: localization of v-src to adhesion plaques is sufficient to transform chicken embryo fibroblasts. Oncogene. 1992 Dec;7(12):2417–2428. [PubMed] [Google Scholar]
- Liu X., Brodeur S. R., Gish G., Songyang Z., Cantley L. C., Laudano A. P., Pawson T. Regulation of c-Src tyrosine kinase activity by the Src SH2 domain. Oncogene. 1993 May;8(5):1119–1126. [PubMed] [Google Scholar]
- Liu X., Marengere L. E., Koch C. A., Pawson T. The v-Src SH3 domain binds phosphatidylinositol 3'-kinase. Mol Cell Biol. 1993 Sep;13(9):5225–5232. doi: 10.1128/mcb.13.9.5225. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MacAuley A., Cooper J. A. The carboxy-terminal sequence of p56lck can regulate p60c-src. Mol Cell Biol. 1988 Aug;8(8):3560–3564. doi: 10.1128/mcb.8.8.3560. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MacAuley A., Okada M., Nada S., Nakagawa H., Cooper J. A. Phosphorylation of Src mutants at Tyr 527 in fibroblasts does not correlate with in vitro phosphorylation by CSK. Oncogene. 1993 Jan;8(1):117–124. [PubMed] [Google Scholar]
- Mayer B. J., Jackson P. K., Van Etten R. A., Baltimore D. Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Mol Cell Biol. 1992 Feb;12(2):609–618. doi: 10.1128/mcb.12.2.609. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meriläinen J., Palovuori R., Sormunen R., Wasenius V. M., Lehto V. P. Binding of the alpha-fodrin SH3 domain to the leading lamellae of locomoting chicken fibroblasts. J Cell Sci. 1993 Jul;105(Pt 3):647–654. doi: 10.1242/jcs.105.3.647. [DOI] [PubMed] [Google Scholar]
- Miller A. D., Miller D. G., Garcia J. V., Lynch C. M. Use of retroviral vectors for gene transfer and expression. Methods Enzymol. 1993;217:581–599. doi: 10.1016/0076-6879(93)17090-r. [DOI] [PubMed] [Google Scholar]
- Miller A. D., Rosman G. J. Improved retroviral vectors for gene transfer and expression. Biotechniques. 1989 Oct;7(9):980-2, 984-6, 989-90. [PMC free article] [PubMed] [Google Scholar]
- Miller A. D., Trauber D. R., Buttimore C. Factors involved in production of helper virus-free retrovirus vectors. Somat Cell Mol Genet. 1986 Mar;12(2):175–183. doi: 10.1007/BF01560664. [DOI] [PubMed] [Google Scholar]
- Murphy S. M., Bergman M., Morgan D. O. Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae. Mol Cell Biol. 1993 Sep;13(9):5290–5300. doi: 10.1128/mcb.13.9.5290. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nada S., Okada M., MacAuley A., Cooper J. A., Nakagawa H. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature. 1991 May 2;351(6321):69–72. doi: 10.1038/351069a0. [DOI] [PubMed] [Google Scholar]
- Nada S., Yagi T., Takeda H., Tokunaga T., Nakagawa H., Ikawa Y., Okada M., Aizawa S. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell. 1993 Jun 18;73(6):1125–1135. doi: 10.1016/0092-8674(93)90642-4. [DOI] [PubMed] [Google Scholar]
- Nigg E. A., Sefton B. M., Hunter T., Walter G., Singer S. J. Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. Proc Natl Acad Sci U S A. 1982 Sep;79(17):5322–5326. doi: 10.1073/pnas.79.17.5322. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Brien M. C., Fukui Y., Hanafusa H. Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain. Mol Cell Biol. 1990 Jun;10(6):2855–2862. doi: 10.1128/mcb.10.6.2855. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Okada M., Howell B. W., Broome M. A., Cooper J. A. Deletion of the SH3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine. J Biol Chem. 1993 Aug 25;268(24):18070–18075. [PubMed] [Google Scholar]
- Okada M., Nada S., Yamanashi Y., Yamamoto T., Nakagawa H. CSK: a protein-tyrosine kinase involved in regulation of src family kinases. J Biol Chem. 1991 Dec 25;266(36):24249–24252. [PubMed] [Google Scholar]
- Okada M., Nakagawa H. A protein tyrosine kinase involved in regulation of pp60c-src function. J Biol Chem. 1989 Dec 15;264(35):20886–20893. [PubMed] [Google Scholar]
- Paige L. A., Nadler M. J., Harrison M. L., Cassady J. M., Geahlen R. L. Reversible palmitoylation of the protein-tyrosine kinase p56lck. J Biol Chem. 1993 Apr 25;268(12):8669–8674. [PubMed] [Google Scholar]
- Parsons J. T., Weber M. J. Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr Top Microbiol Immunol. 1989;147:79–127. doi: 10.1007/978-3-642-74697-0_3. [DOI] [PubMed] [Google Scholar]
- Pawson T., Gish G. D. SH2 and SH3 domains: from structure to function. Cell. 1992 Oct 30;71(3):359–362. doi: 10.1016/0092-8674(92)90504-6. [DOI] [PubMed] [Google Scholar]
- Piwnica-Worms H., Saunders K. B., Roberts T. M., Smith A. E., Cheng S. H. Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell. 1987 Apr 10;49(1):75–82. doi: 10.1016/0092-8674(87)90757-4. [DOI] [PubMed] [Google Scholar]
- Resh M. D. Myristylation and palmitylation of Src family members: the fats of the matter. Cell. 1994 Feb 11;76(3):411–413. doi: 10.1016/0092-8674(94)90104-x. [DOI] [PubMed] [Google Scholar]
- Reynolds A. B., Vila J., Lansing T. J., Potts W. M., Weber M. J., Parsons J. T. Activation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxy terminus. EMBO J. 1987 Aug;6(8):2359–2364. doi: 10.1002/j.1460-2075.1987.tb02512.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rohrschneider L. R. Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3514–3518. doi: 10.1073/pnas.77.6.3514. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Roussel R. R., Brodeur S. R., Shalloway D., Laudano A. P. Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10696–10700. doi: 10.1073/pnas.88.23.10696. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sabe H., Hata A., Okada M., Nakagawa H., Hanafusa H. Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3984–3988. doi: 10.1073/pnas.91.9.3984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sabe H., Knudsen B., Okada M., Nada S., Nakagawa H., Hanafusa H. Molecular cloning and expression of chicken C-terminal Src kinase: lack of stable association with c-Src protein. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2190–2194. doi: 10.1073/pnas.89.6.2190. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sadowski I., Stone J. C., Pawson T. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Mol Cell Biol. 1986 Dec;6(12):4396–4408. doi: 10.1128/mcb.6.12.4396. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Seidel-Dugan C., Meyer B. E., Thomas S. M., Brugge J. S. Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src. Mol Cell Biol. 1992 Apr;12(4):1835–1845. doi: 10.1128/mcb.12.4.1835. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shenoy-Scaria A. M., Gauen L. K., Kwong J., Shaw A. S., Lublin D. M. Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins. Mol Cell Biol. 1993 Oct;13(10):6385–6392. doi: 10.1128/mcb.13.10.6385. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Songyang Z., Shoelson S. E., McGlade J., Olivier P., Pawson T., Bustelo X. R., Barbacid M., Sabe H., Hanafusa H., Yi T. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol Cell Biol. 1994 Apr;14(4):2777–2785. doi: 10.1128/mcb.14.4.2777. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stockschlaeder M. A., Storb R., Osborne W. R., Miller A. D. L-histidinol provides effective selection of retrovirus-vector-transduced keratinocytes without impairing their proliferative potential. Hum Gene Ther. 1991 Spring;2(1):33–39. doi: 10.1089/hum.1991.2.1-33. [DOI] [PubMed] [Google Scholar]
- Superti-Furga G., Fumagalli S., Koegl M., Courtneidge S. A., Draetta G. Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src. EMBO J. 1993 Jul;12(7):2625–2634. doi: 10.1002/j.1460-2075.1993.tb05923.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takeuchi M., Kuramochi S., Fusaki N., Nada S., Kawamura-Tsuzuku J., Matsuda S., Semba K., Toyoshima K., Okada M., Yamamoto T. Functional and physical interaction of protein-tyrosine kinases Fyn and Csk in the T-cell signaling system. J Biol Chem. 1993 Dec 25;268(36):27413–27419. [PubMed] [Google Scholar]
- Twamley-Stein G. M., Pepperkok R., Ansorge W., Courtneidge S. A. The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7696–7700. doi: 10.1073/pnas.90.16.7696. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Verderame M. F., Kaplan J. M., Varmus H. E. A mutation in v-src that removes a single conserved residue in the SH-2 domain of pp60v-src restricts transformation in a host-dependent manner. J Virol. 1989 Jan;63(1):338–348. doi: 10.1128/jvi.63.1.338-348.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wages D. S., Keefer J., Rall T. B., Weber M. J. Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3'-kinase activity with pp60v-src and alter cellular morphology. J Virol. 1992 Apr;66(4):1866–1874. doi: 10.1128/jvi.66.4.1866-1874.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weng Z., Taylor J. A., Turner C. E., Brugge J. S., Seidel-Dugan C. Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells. J Biol Chem. 1993 Jul 15;268(20):14956–14963. [PubMed] [Google Scholar]
- Wu H., Parsons J. T. Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J Cell Biol. 1993 Mar;120(6):1417–1426. doi: 10.1083/jcb.120.6.1417. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wu H., Reynolds A. B., Kanner S. B., Vines R. R., Parsons J. T. Identification and characterization of a novel cytoskeleton-associated pp60src substrate. Mol Cell Biol. 1991 Oct;11(10):5113–5124. doi: 10.1128/mcb.11.10.5113. [DOI] [PMC free article] [PubMed] [Google Scholar]