Presence of an SH2 Domain in the Actin-Binding Protein Tensin

Davis, Samuel; Lu, Michael L.; Lo, Su Hao; Lin, Shin; Butler, James A.; Druker, Brian J.; Roberts, Thomas M.; An, Qing; Chen, Lan Bo

doi:10.1126/science.1708917

Cited by 239 publications

(152 citation statements)

References 31 publications

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“…Tensin includes both phosphorylated tyrosine residues and a Src homology 2 (SH2) domain, which is shared by a number of signal transduction proteins [34]. It is suggested that tensin may link signal transduction pathways with the cytoskeleton by possessing both actin-binding and phosphotyrosine-binding properties and being itself a target for tyrosine kinases [35]. Since GAK also has tensin-like properties such as an actin-binding domain and a target site for tyrosine kinases, it is conceivable that GAK plays a similar role in the cytoskeletal signal transduction pathway.…”

Section: Discussionmentioning

confidence: 99%

“…In the middle part of the molecule (Fig. 1C), GAK resembles both tensin, an actin-binding component of adhesion plaques (also called focal contacts) and other submembranous cytoskeletal structures [16], and auxilin, a coat component of brain clathrin-coated vesicles [17,18]. The domain homologous to tensin and auxilin (we call it the TAG domain hereafter) occupies more than half of the whole molecule and contains, in addition, a leucine zipper region [19] in the C-terminal portion of this domain.…”

Section: Molecular Cloning Of Gakmentioning

confidence: 99%

“…Structure of GAK. A: Schematic presentation of the structure of rat GAK, tensin [16] and auxilin [17]. The consensus domain for Ser/ Thr kinases (filled box), the conserved domains between GAK and auxilin (shaded box), and homologous regions between GAK, tensin and auxilin (TAG domain as stippled box) are indicated.…”

Section: Characterization Of the Antibodiesmentioning

confidence: 99%

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GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain¹

Kanaoka

Kimura

Okazaki³

et al. 1997

FEBS Letters

123

166

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We have cloned a cDNA encoding a novel association partner of cyclin G by West-Western blotting. The cDNA encodes a protein that harbors a Ser/Thr protein kinase-like catalytic domain at the N-terminal. Hence, we named it GAK (cyclin G-associated kinase). The long C-terminal extension shares homology with tensin and auxilin, and contains a leucine zipper region. Co-immunoprecipitation and Western blotting showed that GAK and cyclin G associate together in vivo. GAK also co-precipitated with CDK5, and CDK5 was found to be associated with cyclin G. We also showed by BIAcore analysis that the GAK-cyclin G interaction was direct.

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Section: Discussionmentioning

confidence: 99%

Section: Molecular Cloning Of Gakmentioning

confidence: 99%

See 1 more Smart Citation

GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain¹

Kanaoka

Kimura

Okazaki³

et al. 1997

FEBS Letters

123

166

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“…Tyrosine phosphorylation of tensin (Davis et al, 1991), talin (DeClue and Marin, 1987), p120 (Kanner et al, 1990;Reynolds et al, 1992), p80/85 (cortactin) (Wu et al, 1991) and paxillin (Turner et al, 1990) was greatly reduced or became almost undetectable when the cell to substratum adhesion was lost (Figure 2). Tyrosine phosphorylation of these proteins was then restored to similar to the original levels when the cells in suspension were spread on ®bronectin-coated culture dishes in the absence of serum (Figure 2).…”

Section: Resultsmentioning

confidence: 99%

Cell to substratum adhesion is involved in v-Src-induced cellular protein tyrosine phosphorylation: implication for the adhesion-regulated protein tyrosine phosphatase activity

1997

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Protein tyrosine phosphorylation accompanies the integrin-mediated cell to substratum adhesion, and is essential for the progression of G 1 /S phase of the cellcycle in normal ®broblasts. To examine how cellular protein tyrosine phosphatase (PTPase) activity is involved in regulating the adhesion-dependent protein tyrosine phosphorylation, we employed ®broblast cells bearing an active form of a protein tyrosine kinase (PTK), v-Src. We found that the v-Src induced tyrosine phosphorylation in certain proteins such as tensin, talin, p120, p80/85 (cortactin) and paxillin was greatly reduced when the cell to substratum adhesion was lost. Readhesion of the cells onto ®bronectin restored these phosphorylation events, while this was inhibited by the addition of RGD peptide. The kinase activity of the v-Src was unchanged by the loss of cell to substratum adhesion. On the other hand, treatment with a protein tyrosine phosphatase inhibitor vanadate caused much the same increase in the v-Src-mediated cellular tyrosine phosphorylation between cells adhered to the culture environments and cells kept in suspension. These data suggest that PTPase(s) appears to be more critical than the v-Src PTK in determining the cell adhesion-dependent protein tyrosine phosphorylation. Moreover, most of the protein tyrosine phosphorylations that are mediated by the v-Src but still dependent on the cell adhesion were indeed greatly reduced during an anchorage-independent growth of v-Src cells. Thus our data collectively indicate that the v-Src induced high level of tyrosine phosphorylation in certain types of proteins are still under the control of the integrin(s) or the cell adhesion to culture substratum, and most of these adhesion-regulated high levels of tyrosine phosphorylations are not essential for the transformed phenotype.

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“…These proteins may have signal protein binding domains such as SH2 and SH3 domains (Feller et al, 1994) or binding motifs for these domains, or they may bind adaptor proteins which link them to signaling proteins (Feller et al, 1994;Birge et al, 1996). For example, the actinbinding protein tensin (Lo et al, 1994a) contains an SH2 domain (Davis et al, 1991), implicating this membrane skeletal protein in linking signal transduction to the cytoskeleton (Lo et al, 1994b). Although their cellular functions are yet poorly understood, SH3 domains have also been strongly implicated in cellular localization of signaling elements to activated receptors and to the membrane-cytoskeleton interface .…”

Section: Introductionmentioning

confidence: 99%

c-Src association with and phosphorylation of p58gag, a membrane- and microfilament-associated retroviral Gag-like protein in a xenotransplantable rat mammary tumor

Huang

Zhang

et al. 1999

Oncogene

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The retroviral Gag-like protein p58 gag expressed in a highly metastatic ascites rat mammary adenocarcinoma has been implicated in cell surface changes contributing to xenotransplantability. p58 gag is present in the cells in a plasma membrane-and micro®lament-associated signal transduction particle containing Src and is phosphorylated on tyrosine. Overlay analyses and a nity chromatography with glutathione S-transferase (GST) fusion proteins of Src homology-3 (SH3) domains showed direct binding of the Src but not the Crk SH3 domain to p58 gag . This association was con®rmed by coimmunoprecipitation of partially puri®ed p58 gag from ascites cell lysates with platelet Src. Further, a GSTp58 gag fusion protein bound full length c-Src from either platelets or c-Src-expressing insect cells. The GST-p58 gag fusion protein, but not GST, was phosphorylated by platelet or insect cell-expressed c-Src, but not by a kinase negative c-Src variant. The binding of GST-p58 gag to c-Src was almost completely abolished by a 50-fold excess of the GST-SH3 domain of Src, and a parallel decrease in tyrosine phosphorylation of p58 gag was observed. These results demonstrate that p58 gag is tyrosine-phosphorylated as a consequence of its speci®c association with c-Src via its SH3 domain. These observations suggest a mechanism by which Gag proteins may contribute to retroviral maturation or pathogenesis through binding and relocalization of SH3 domaincontaining proteins such as Src-like tyrosine kinases to sites of association of micro®laments with the plasma membrane.

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Presence of an SH2 Domain in the Actin-Binding Protein Tensin

Cited by 239 publications

References 31 publications

GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain¹

GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain¹

Cell to substratum adhesion is involved in v-Src-induced cellular protein tyrosine phosphorylation: implication for the adhesion-regulated protein tyrosine phosphatase activity

c-Src association with and phosphorylation of p58gag, a membrane- and microfilament-associated retroviral Gag-like protein in a xenotransplantable rat mammary tumor

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Presence of an SH2 Domain in the Actin-Binding Protein Tensin

Cited by 239 publications

References 31 publications

GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain1

GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain1

Cell to substratum adhesion is involved in v-Src-induced cellular protein tyrosine phosphorylation: implication for the adhesion-regulated protein tyrosine phosphatase activity

c-Src association with and phosphorylation of p58gag, a membrane- and microfilament-associated retroviral Gag-like protein in a xenotransplantable rat mammary tumor

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GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain¹

GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain¹