Rab (G-protein)

The Rab family of proteins is a member of the Ras superfamily of small G proteins.[1] Approximately 70 types of Rabs have now been identified in humans.[2] Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helices.[3] Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside the cell, such as the transferrin receptor, or serves as a means of regulating the number of a certain type of protein molecules on the surface.

  1. ^ Stenmark H, Olkkonen VM (2001). "The Rab GTPase family". Genome Biology. 2 (5): REVIEWS3007. doi:10.1186/gb-2001-2-5-reviews3007. PMC 138937. PMID 11387043.
  2. ^ Seto, Shintaro; Tsujimura, Kunio; Horii, Toshinobu; Koide, Yukio (2014-01-01), Hayat, M. A. (ed.), "Chapter 10 - Mycobacterial Survival in Alveolar Macrophages as a Result of Coronin-1a Inhibition of Autophagosome Formation", Autophagy: Cancer, Other Pathologies, Inflammation, Immunity, Infection, and Aging, Amsterdam: Academic Press, pp. 161–170, doi:10.1016/b978-0-12-405877-4.00010-x, ISBN 978-0-12-405877-4, retrieved 2020-11-19
  3. ^ Hutagalung AH, Novick PJ (January 2011). "Role of Rab GTPases in membrane traffic and cell physiology". Physiological Reviews. 91 (1): 119–49. doi:10.1152/physrev.00059.2009. PMC 3710122. PMID 21248164.