Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase.
作者： C.F. Albright , B.W. Giddings , J. Liu , M. Vito , R.A. Weinberg
DOI: 10.1002/J.1460-2075.1993.TB05662.X
关键词:
摘要: ras-related GTPases participate in signaling for a variety of cellular processes. The cycle between GTP-bound active state and GDP-bound inactive state. This cycling is partially controlled by guanine nucleotide dissociation stimulators (GDS, also known as exchange factors). We report on the molecular cloning cDNAs encoding new mammalian GDS protein, using sequences derived from yeast ras proteins probes. encoded protein stimulates nucleotides ralA ralB at rate least 30-fold faster than intrinsic rate. GDS, ralGDS, 20-fold more any other GTPase tested, including members family (H-ras, N-ras, K-ras, R-ras, rap1a rap2), rho (rhoA, rhoB CDC42-Hs) rab (rab3a ypt1). While ralGDS phosphorylated serine residues, we find no evidence that phosphorylation affects activity insect cell-expressed towards or GTPase. 3600 mRNA 115 kDa were found all tissues cell lines examined.
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