Abstract:
:The neurofibromatosis type 1 (NF1) protein contains a region of significant sequence similarity to ras p21 GTPase-activating protein (GAP) and the yeast IRA1 gene product. A fragment of NF1 cDNA encoding the GAP-related domain (NF1 GRD) was expressed, immunoaffinity purified, and assayed for effects on N-ras p21 GTPase activity. The GTPase of wild-type ras p21 was stimulated by NF1 GRD, but oncogenic mutants of ras p21 (Asp-12 and Val-12) were unaffected, and the GTPase of an effector mutant (Ala-38) was only weakly stimulated. NF1 GRD also down-regulated RAS function in S. cerevisiae. The affinity of NF1 GRD for ras p21 was estimated to be 250 nM: this is more than 20-fold higher than the affinity of GAP for ras p21. However, its specific activity was about 30 times lower. These kinetic measurements suggest that NF1 may be a significant regulator of ras p21 activity, particularly at low ras p21 concentrations.
journal_name
Celljournal_title
Cellauthors
Martin GA,Viskochil D,Bollag G,McCabe PC,Crosier WJ,Haubruck H,Conroy L,Clark R,O'Connell P,Cawthon RMdoi
10.1016/0092-8674(90)90150-dsubject
Has Abstract,Author List Incompletepub_date
1990-11-16 00:00:00pages
843-9issue
4eissn
0092-8674issn
1097-4172pii
0092-8674(90)90150-Djournal_volume
63pub_type
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