The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells (Q28180409)

A disintegrin and metallopeptidase domain 19 (meltrin beta)

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

fish

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author name string

Clare L Abram

1

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Darren F Seals

2

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Ian Pass

3

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Daniel Salinsky

4

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Lisa Maurer

5

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Therese M Roth

6

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Sara A Courtneidge

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

9 May 2003

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published in

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volume

278

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issue

19

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page(s)

16844-51

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cites work

A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate

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Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains?

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Location, location, location: membrane targeting directed by PX domains

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Solution structure of the PX domain, a target of the SH3 domain

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The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate

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Altered distributions of the cytoskeletal proteins vinculin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus

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Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes

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Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells

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The ADAMs family of metalloproteases: multidomain proteins with multiple functions

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The ADAM gene family: surface proteins with adhesion and protease activity

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Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells

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Characterisation of a plant 3-phosphoinositide-dependent protein kinase-1 homologue which contains a pleckstrin homology domain

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The PX domains of p47phox and p40phox bind to lipid products of PI(3)K

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PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40phox

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Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.

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Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides

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The Phox homology (PX) domain, a new player in phosphoinositide signalling

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Trafficking of human ADAM 12-L: retention in the trans-Golgi network

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All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate.

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Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47(phox), thereby acti

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Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction

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A novel protease-docking function of integrin at invadopodia

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Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion

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Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility

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Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells

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Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization

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Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells

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Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src

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Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1

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Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases

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Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion

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A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.

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