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Synthetic peptides of the Rab effector domain inhibit vesicular transport through the secretory pathway.
Author(s) -
Plutner H.,
Schwaninger R.,
Pind S.,
Balch W. E.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb07412.x
Subject(s) - biology , rab , effector , vesicular transport protein , microbiology and biotechnology , transport protein , secretory pathway , secretion , domain (mathematical analysis) , vesicular transport proteins , computational biology , biochemistry , vesicle , peptide sequence , gtpase , golgi apparatus , n terminus , gene , endoplasmic reticulum , membrane , mathematical analysis , mathematics
Synthetic peptides of the putative effector domain of members of the ras‐related rab gene family of small GTP‐binding proteins were synthesized and found to be potent inhibitors of endoplasmic reticulum (ER) to Golgi and intra‐Golgi transport in vitro. Inhibition of transport by one of the effector domain peptides was rapid (t1/2 of 30 s), and irreversible. Analysis of the temporal site of peptide inhibition indicated that a late step in transport was blocked, coincident with a Ca2(+)‐dependent prefusion step. The results provide novel biochemical evidence for the role of members of the rab gene family in vesicular transport in mammalian cells, and implicate a role for a new downstream Rab effector protein (REP) regulating vesicle fusion.