Journal
MOLECULAR CELL
Volume 9, Issue 1, Pages 85-94Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00432-4
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Funding
- NATIONAL CANCER INSTITUTE [R01CA072971] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [T32HL007781] Funding Source: NIH RePORTER
- NCI NIH HHS [CA072971-04] Funding Source: Medline
- NHLBI NIH HHS [T32 HL07781] Funding Source: Medline
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In fibroblast cells, cAMP antagonizes growth factor activation of ERKs and cell growth via PKA and the small G protein Rap1. We demonstrate here that PKA's activation of Rap1 was mediated by the Rap1 guanine nucleotide exchange factor C3G, the adaptor Crk-L, the scaffold protein Cbl, and the tyrosine kinase Src. Src was required for cAMP activation of Rap1 and the inhibition of ERKs and cell growth. PKA activated Src both in vitro and in vivo by phosphorylating Src on serine 17 within its amino terminus. This phosphorylation was required for cAMP's activation of Src and Rapt, as well as cAMP's inhibition of ERKs and cell proliferation. This study identifies an antiproliferative role for Src in the physiological regulation of cell growth by cAMP.
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