Regulation of chemotaxis by the platelet-derived growth factor receptor-β View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-02

AUTHORS

V Kundra, J A Escobedo, A Kazlauskas, H K Kim, S G Rhee, L T Williams, B R Zetter

ABSTRACT

Chemotaxis is an important component of wound healing, development, immunity and metastasis, yet the signalling pathways that mediate chemotaxis are poorly understood. Platelet-derived growth factor (PDGF) acts both as a mitogen and a chemoattractant. Upon stimulation, the tyrosine kinase PDGF receptor-beta (PDGFR-beta) autophosphorylates and forms a complex that includes SII2(Src homology 2)-domain-containing proteins such as the phosphatidylinositol-specific phospholipase C-gamma, Ras-GTPase-activating protein (GAP), and phosphatidylinositol-3-OH kinase. Specific tyrosine-to-phenylalanine substitutions in the PDGFR-beta can prevent binding of one SH2-domain-containing protein without affecting binding of other receptor-associated proteins. Here we use phospholipase C-gamma and PDGFR-beta mutants to map specific tyrosines involved in both positive and negative regulation of chemotaxis towards the PDGF-BB homodimer. Our results indicate that a delicate balance of migration-promoting (phospholipase C-gamma and phosphatidylinositol-3-OH kinase) and migration-suppressing (GAP) activities are recruited by the PDGFR-beta to drive chemotaxis towards PDGF-BB. More... »

PAGES

474-476

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/367474a0

DOI

http://dx.doi.org/10.1038/367474a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030955834

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8107807


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