An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation (Q78112212)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10442635%20AND%20SRC:MED&resulttype=core&format=json

11 December 2019

title

An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation (English)

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11 December 2019

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Bowden ET

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11 December 2019

Barth M

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11 December 2019

Thomas D

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11 December 2019

Glazer RI

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11 December 2019

Mueller SC

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11 December 2019

language of work or name

English

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publication date

1 August 1999

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11 December 2019

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11 December 2019

volume

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11 December 2019

issue

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11 December 2019

page(s)

4440-4449

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Differential effects of platelet-derived growth factor BB on p125 focal adhesion kinase and paxillin tyrosine phosphorylation and on cell migration in rabbit aortic vascular smooth muscle cells and Swiss 3T3 fibroblasts

11 December 2019

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Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly

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Integrin alpha 3 beta 1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells

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Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase

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The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells

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Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation.

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Invadopodia promote proteolysis of a wide variety of extracellular matrix proteins.

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Receptor tyrosine kinase signaling required for integrin alpha v beta 5-directed cell motility but not adhesion on vitronectin

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Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation

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Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells

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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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A mechanism for regulation of melanoma invasion. Ligation of alpha6beta1 integrin by laminin G peptides

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p80/85 Cortactin Associates with the Src SH2 Domain and Colocalizes with v-Src in Transformed Cells

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Overexpression of EMS1/cortactin in NIH3T3 fibroblasts causes increased cell motility and invasion in vitro

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Protein kinase C mu is located at the Golgi compartment

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The product of the EMS1 gene, amplified and overexpressed in human carcinomas, is homologous to a v-src substrate and is located in cell-substratum contact sites

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7 January 2021

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