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The small GTP-binding protein rab4 is associated with early endosomes

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
; ;  [1]; ;  [2];  [3]
  1. Yale Univ. School of Medicine, New Haven, CT (United States)
  2. INSERM U 248, Paris (France)
  3. Unite de Genetique Somatique, Paris (France)

Small GTP-binding proteins of the rab family have been implicated as playing important roles in controlling membrane traffic on the biosynthetic and endocytic pathways. The authors demonstrate that a distinct rab protein, rab4p, is associated with the population of early endosomes involved in transferrin-receptor recycling. An antibody to human rab4p was found to detect a doublet of {approx} 24-kDa proteins on immunoblots from various cell types. Seventy-five percent of these proteins were tightly membrane bound and could be released only by detergent treatment. Upon isolation of early endosomes, late endosomes, and lysosomes, by free-flow electrophoresis and Percoll density-gradient centrifugation, most (70%) of the rab4p was found to cofractionate with early endosomes and endocytic vesicles containing {sup 125}-labeled transferrin. The rab proteins previously localized to the endoplasmic reticulum and/or Golgi apparatus were not found in these fractions. They also localized rab4p to tansferrin-receptor-containing early endosomes by immunofluorescence after expression of rab4p cDNA. The association of rab4p with early endosomes and other vesicles involved in the intracellular tansport of transferrin receptor suggests that rab4p may play a role in regulating the pathway of receptor recycling.

OSTI ID:
6096682
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 88:14; ISSN PNASA; ISSN 0027-8424
Country of Publication:
United States
Language:
English