| First Author | Albright CF | Year | 1993 |
| Journal | EMBO J | Volume | 12 |
| Issue | 1 | Pages | 339-47 |
| PubMed ID | 8094051 | Mgi Jnum | J:25192 |
| Mgi Id | MGI:72921 | Doi | 10.1002/j.1460-2075.1993.tb05662.x |
| Citation | Albright CF, et al. (1993) Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase. EMBO J 12(1):339-47 |
| abstractText | ras-related GTPases participate in signaling for a variety of cellular processes. The GTPases cycle between a GTP-bound active state and a 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 of cDNAs encoding a new mammalian GDS protein, using sequences derived from the yeast ras GDS proteins as probes. The encoded protein stimulates the dissociation of guanine nucleotides from the ras-related ralA and ralB GTPases at a rate at least 30-fold faster than the intrinsic nucleotide dissociation rate. This new GDS, ralGDS, is at least 20-fold more active on the ralA and ralB GTPases than on any other GTPase tested, including other members of the ras family (H-ras, N-ras, K-ras, R-ras, rap1a and rap2), members of the rho family (rhoA, rhoB and CDC42-Hs) and members of the rab family (rab3a and ypt1). While the ralGDS protein is phosphorylated on serine residues, we find no evidence that phosphorylation affects the activity of insect cell-expressed ralGDS towards the ralA or ralB GTPase. The 3600 nucleotide ralGDS mRNA and the 115 kDa protein were found in all tissues and cell lines examined. |
