Purification, crystallization and preliminary X-ray analysis of the GTP-binding protein Rab9 implicated in endosome-to-TGN vesicle trafficking.
Rab GTP-binding proteins are involved in the regulation of distinct vesicular-transport events involving membrane targeting and fusion. They differ from other small GTPases by the presence of specific loop regions that serve as effector-binding sites in addition to the classical switch I and switch II regions. While the structures of many small GTP-binding proteins of the Ras superfamily are available in both GDP- and GTP-bound forms, Rab proteins are less well characterized than Ras proteins at the structural level. The crystallization of Rab9, a key regulatory component in the recycling of mannose-6-phosphate receptors from endosomes to the trans-Golgi network, is described here.
Wittmann
Julia G
JG
Molecular Structural Biology, University of Göttingen, Justus-von-Liebig-Weg 11, Goettingen D-37077, Germany.
Rudolph
Markus G
MG
D000818:Animals; D001693:Biological Transport, Active / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004285:Dogs; D011992:Endosomes / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism*; D011485:Protein Binding; D017527:Receptor, IGF Type 2 / Q000378:metabolism; D020691:rab GTP-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D018631:ras Proteins / Q000378:metabolism; D021601:trans-Golgi Network / Q000378:metabolism*
D017527:Receptor, IGF Type 2; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D020691:rab GTP-Binding Proteins; D018631:ras Proteins