Cellular functions of the Rap1 GTP-binding protein: a pattern emerges.
Rap1 belongs to the Ras subgroup of small GTP-binding proteins. Whereas its early history has focused on its biochemical homology to Ras and the alleged functional antagonism between these two small GTPases, recent cellular evidence suggests that endogenous Rap1 plays a unique, Ras-independent role in eukaryotic cells. Activated by virtually all receptor types and second messengers, Rap1 controls adhesion-related functions such as phagocytosis, cell-cell contacts and functional activation of integrins through inside-out signalling. Whereas the precise mechanism by which its downstream effectors exert these diverse functions is unknown, Rap1 seems to fulfil the evolutionarily conserved function of patterning the eukaryotic cell, thus enabling it to respond to its environment, in particular through cytoskeletal remodelling.
Caron
Emmanuelle
E
Department of Biological Sciences, The Flowers Building, Room 2:41, Armstrong Road, Imperial College of Science, Technology and Medicine, London SW7 2AZ, UK. e.caron@ic.ac.uk
D000818:Animals; D002448:Cell Adhesion / Q000235:genetics*; D002450:Cell Communication / Q000235:genetics*; D003599:Cytoskeleton / Q000378:metabolism; D005057:Eukaryotic Cells / Q000201:enzymology*; D006801:Humans; D015290:Second Messenger Systems / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000235:genetics; D020827:rap1 GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*
D020827:rap1 GTP-Binding Proteins