Characterization of a membrane‐associated glycoprotein complex implicated in cell adhesion to fibronectin

Hasegawa, Takayuki; Hasegawa, Eiichi; Chen, Wen-Tien; Yamada, Kenneth M.

doi:10.1002/jcb.240280409

Cited by 93 publications

(61 citation statements)

References 28 publications

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“…Recently, several laboratories have identified an additional adhesion-plaque protein complex with properties consistent with its being a receptor for extracellular matrix proteins (22)(23)(24)(25)(26)(27)(28)(29)(30). In vitro experiments have demonstrated a direct association between this complex and FN (30-31).…”

Section: Introductionmentioning

confidence: 99%

“…It was initially speculated that vinculin linked stress fibers to the plasma membrane within focal contacts (7), and the increased phosphorylation of vinculin on its tyrosine residues might be responsible for the general decrease of stress-fiber organization seen in these transformed cells (17). Although attractive, the phosphorylation of vinculin was not related to actin cable organization (18)(19)(20), and it is possible that the phosphorylation of tyrosine in vinculin and several other cellular substrates of pp60S1 is simply a fortuitous event (21).Recently, several laboratories have identified an additional adhesion-plaque protein complex with properties consistent with its being a receptor for extracellular matrix proteins (22)(23)(24)(25)(26)(27)(28)(29)(30). In vitro experiments have demonstrated a direct association between this complex and FN (30-31).…”

mentioning

confidence: 99%

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Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases.

Hirst¹,

Horwitz²,

Buck³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

322

191

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The fibronectin (FN) receptor in avian cells has been characterized previously as a complex of three membrane glycoproteins of about Mr 160,000, Mr 140,000, and Mr 120,000 (simply termed protein band 1, band 2, and band 3, respectively). Monoclonal antibodies to the band 3 protein of the complex prevent FN and laminin binding both in vivo and in vitro and enable the detection of the receptor proteins in the plasma membrane and in adhesion plaques. Association of the FN receptor proteins with the adhesion-plaque protein talin also has been reported. We now find that the band 2 and band 3 proteins in the complex are phosphorylated in Rous sarcoma virus-transformed chicken cells but not in normal chicken cells. Phosphorylation occurs predominantly on tyrosine and is accompanied by a reorganization ofthe receptor complex in the membrane of the transformed cells. Whereas normal cells contain the FN receptor in focal contacts and cellular processes between cells, v-src-transformed cells exhibit a more diffuse distribution of this receptor. In addition to the viral v-src oncogene, cells transformed by other avian oncogenes that also encode tyrosine kinases (v-.fs, v-erbB, and v-yes) also express the receptor complex proteins in the phosphorylated state regardless of whether the transforming protein is detectable in adhesion plaques. These results suggest that the altered FN and laminin receptor proteins may contribute to the transformed phenotype, but their significance and role in the transformed state remain to be established.Transformation by Rous sarcoma virus (RSV) is initiated and maintained by the protein product of the viral v-src gene (1, 2). This protein, designated pp60src, possesses an inherent tyrosine kinase activity essential for transformation and is situated along the cytoplasmic face of the plasma membrane and concentrated within cell-substratum adhesion sites (3). These latter sites are termed focal contacts or adhesion plaques and are associated either directly or indirectly with several functions that are altered in RSV-transformed cells. Focal contacts mediate not only the physical associations of cells to each other and to substrata (via extracellular molecules) but also serve as organizing centers for attachment of extracellular matrix protein and intracellular focal points for stress-fiber termination (4-10). These sites are very specialized regions of the plasma membrane, and proteins within these structures are logical targets for such RSV-induced alterations as decreased cellular adhesiveness, loss of cell surface fibronectin (FN), abnormal cell migration, dissolution of stress-fiber bundles, and ultimately the rounded transformed cell morphology.Little is known of the molecular composition and complexity of adhesion plaques; however, several proteins have been identified as constituents of these structures (7,(11)(12)(13)(14)(15)(16).Of these proteins, vinculin has received considerable attention because it was shown to contain increased levels of phosphotyrosine in RSV-transformed...

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Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases.

Hirst¹,

Horwitz²,

Buck³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

322

191

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“…In vitro studies indicate that glycoprotein GPIIb-IIIa, a member of a family of adhesion receptors called integrins, exists on the surface of endothelial cells (33). Integrins are transmembrane glycoproteins known to bind both extracellular matrix components, such as fibronectin (10,21), laminin (10), and vitronectin (10), and cytoskeletal proteins, such as talin and vinculin (23), in adhesion plaques. Although plaque structures have not been observed in endothelium in vivo, the cytoplasmic aspect of endothelial cell junctions does include a dense peripheral band of actin filaments which is associated with vinculin (40).…”

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confidence: 99%

A CD44-like endothelial cell transmembrane glycoprotein (GP116) interacts with extracellular matrix and ankyrin.

Bourguignon

Lokeshwar

et al. 1992

Mol. Cell. Biol.

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We used complementary biochemical and immunological techniques to establish that an endothelial cell transmembrane glycoprotein, GP116, is a CD44-like molecule and binds directly both to extracellular matrix components (e.g., hyaluronic acid) and to ankyrin. The specific characteristics of GP116 are as follows: (i) GP116 can be surface labeled with Na125I and contains a wheat germ agglutinin-binding site(s), indicating that it has an extraceHlular domain; (ii) GP116 displays immunological cross-reactivity with a panel of CD44 antibodies, shares some peptide similarity with CD44, and has a similar 52-kDa precursor molecule, indicating that it is a CD44-like molecule; (iii) GP116 displays specific hyaluronic acid-binding properties, indicating that it is a hyaluronic acid receptor; (iv) GP116 can be phosphorylated by endogenous protein kinase C activated by 12-O-tetradecanoylphorbol-13-acetate and by exogenously added protein kinase C; and (v) GP116 and a 20-kDa tryptic polypeptide fragment of GP116 from the intracellular domain are capable of binding the membrane-cytoskeleton linker molecule, ankyrin. Furthermore, phosphorylation of GP116 by protein kinase C significantly enhances GP116 binding to ankyrin. Together, these findings strongly suggest that phosphorylation of the transmembrane glycoprotein GP116 (a CD44-like molecule) by protein kinase C is required for effective GP116-ankyrin interaction during endothelial cell adhesion events.

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“…It has been proposed that the pp60src kinase with several different polyclonal and monoclonal exerts its effects through phosphorylation of antibodies [26,27]. No differences in pattern of various proteins, such as the fibronectin receptor, receptor subunits could be detected between vinculin and talin.…”

Section: Resultsmentioning

confidence: 99%

The migratory behavior of avian embryonic cells does not require phosphorylation of the fibronectin‐receptor complex

et al. 1988

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When locomotory embryonic cells become stationary, they acquire new substratum-adhesion properties. In particular, the distribution of fibronectin receptors shifts from diffuse and highly mobile on the cell membrane to immobilized in close association with fibronectin molecules and cytoskeletal elements in focal contacts. Receptor phosphorylation has been proposed as a possible regulator of the interaction between the receptor and its intracellular and extracellular ligands. In the present study, we have compared the phosphorylation state of the fibronectin receptor in motile neural crest and somitic cells, in stationary somitic cells, and in Rous-sarcoma virus transformed-chick embryo fibroblasts, using immunoprecipitation following metabolic labeling. While no receptor phosphorylation was detected in motile embryonic cells, the beta subunit of the receptor was phosphorylated in stationary cells. This subunit was also highly phosphorylated in Rous-sarcoma virus-transformed chicken cells. These results suggest that phosphorylation of the fibronectin receptor cannot account for its distribution in the cell membrane and for the nature of the interactions between this receptor and its ligands in embryonic cells.

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Characterization of a membrane‐associated glycoprotein complex implicated in cell adhesion to fibronectin

Cited by 93 publications

References 28 publications

Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases.

Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases.

A CD44-like endothelial cell transmembrane glycoprotein (GP116) interacts with extracellular matrix and ankyrin.

The migratory behavior of avian embryonic cells does not require phosphorylation of the fibronectin‐receptor complex

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