Literature DB >> 16757332

Phospholipase Cepsilon guanine nucleotide exchange factor activity and activation of Rap1.

Takaya Satoh1, Hironori Edamatsu, Tohru Kataoka.   

Abstract

Phospholipase C (PLC) epsilon is directly regulated by Ras and Rap1 small GTPases: Ras and Rap1, in their GTP-bound form, interact with the Ras/Rap1-associationg (RA) domain of PLCepsilon, thereby translocating PLCepsilon to the plasma membrane and the Golgi apparatus, respectively. In the plasma membrane and the Golgi apparatus, PLCepsilon acts as a phosphoinositide-specific PLC, regulating various downstream signaling pathways. PLCepsilon also contains a CDC25 homology domain, which enhances guanine nucleotide exchange on Rap1. Here, we describe biochemical characterization of the CDC25 homology domain of PLCepsilon and provide insights into its physiological role in the regulation of PLCepsilon activity.

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Year:  2006        PMID： 16757332     DOI： 10.1016/S0076-6879(05)07024-2

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN： 0076-6879            Impact factor:   1.600


  10 in total

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  10 in total

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