4.4 Article

Human VPS34 and p150 are rab7 interacting partners

Journal

TRAFFIC
Volume 4, Issue 11, Pages 754-771

Publisher

WILEY
DOI: 10.1034/j.1600-0854.2003.00133.x

Keywords

endocytosis; membrane trafficking; phosphatidylinositol 3 '-kinase; phosphoinositides; vesicular transport

Categories

Funding

  1. NATIONAL CANCER INSTITUTE [R24CA088339] Funding Source: NIH RePORTER
  2. NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR011830, S10RR016918, S10RR014668] Funding Source: NIH RePORTER
  3. NCI NIH HHS [R24 CA88339] Funding Source: Medline
  4. NCRR NIH HHS [RR11830, S10 RR016918, S10 RR14668] Funding Source: Medline

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Regulation of membrane trafficking requires the concerted actions of rab proteins, their effectors and several phosphatidylinositol 3'-kinases. Rab7 is required for late endosomal transport and here we establish that the phosphatidylinositol 3'-kinase hVPS34 and its adaptor protein p150 are rab7 interacting partners. The hVPS34/p150 complex colocalized with rab7 on late endosomes and hVPS34 activity was dependent on nucleotide cycling of rab7. In addition, total cellular phosphatidylinositol 3'-phosphate levels were modulated by rab7 expression, suggesting that rab7 activation impacted kinase cycling to early endosomes. The data identify rab7 as an important regulator of late endosomal hVPS34 function and link rab7 to the regulation of phosphatidylinositol 3'-kinase cycling between early and late endosomes.

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