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Chemical-genetic inhibition of a sensitized mutant myosin Vb demonstrates a role in peripheral-pericentriolar membrane traffic.

Authors: Provance, D William  Gourley, Christopher R  Silan, Colleen M  Cameron, L C  Shokat, Kevan M  Goldenring, James R  Shah, Kavita  Gillespie, Peter G  Mercer, John A 
Citation: Provance DW, etal., Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1868-73. Epub 2004 Feb 6.
Pubmed: (View Article at PubMed) PMID:14766983
DOI: Full-text: DOI:10.1073/pnas.0305895101

Selective, in situ inhibition of individual unconventional myosins is a powerful approach to determine their specific physiological functions. Here, we report the engineering of a myosin Vb mutant that still hydrolyzes ATP, yet is selectively sensitized to an N(6)-substituted ADP analog that inhibits its activity, causing it to remain tightly bound to actin. Inhibition of the sensitized mutant causes inhibition of accumulation of transferrin in the cytoplasm and increases levels of plasma-membrane transferrin receptor, suggesting that myosin Vb functions in traffic between peripheral and pericentrosomal compartments.


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RGD Object Information
RGD ID: 13461756
Created: 2017-11-25
Species: All species
Last Modified: 2017-11-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.