High impact information on Rab34

• Although wild-type Rah exhibited extremely low GTPase activity in vitro, it exerted appreciable GTPase activity in vivo [1].
• In fibroblasts, Rah was colocalized with actin to the membrane ruffles and membranes of relatively large vesicles adjacent to the ruffles [1].
• Rah was predominantly associated with nascent macropinosomes, whereas Rab5 was present in endosomes at later stages [1].
• The function of Rab34 in macropinosome formation is analyzed by the transfection of wild-type, constitutively active, and dominant-negative mutants of Rab34 in fibroblasts followed by treatment with platelet-derived growth factor (PDGF) or phorbol ester [2].

Biological context of Rab34

• Rab34 lacks a consensus sequence of the fourth motif for GTP/GDP binding and GTPase activities [2].

References