Protein kinase Cepsilon is localized to the Golgi via its zinc-finger domain and modulates Golgi function

Protein kinase Cepsilon is localized to the Golgi via its zinc-finger domain and modulates Golgi function

NIH 3T3 cells were stably transfected to overexpress different epitope-tagged fragments of protein kinase C (PKC) epsilon to examine the interrelationship between the biological effects and domain structure of PKCepsilon. PKCepsilon domains other than the kinase domain may also have biological activ...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS Vol. 92; no. 5; p. 1406
Main Authors: Lehel, Csaba, Olah, Zoltan, Jakab, Gabor, Anderson, Wayne B
Format: Journal Article
Language:English
Published: Washington National Academy of Sciences 28-02-1995
Subjects:
Biochemistry
Cellular biology
Proteins
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Summary:NIH 3T3 cells were stably transfected to overexpress different epitope-tagged fragments of protein kinase C (PKC) epsilon to examine the interrelationship between the biological effects and domain structure of PKCepsilon. PKCepsilon domains other than the kinase domain may also have biological activity, and the zinc-finger domain may function as a subcellular localization signal.
ISSN:0027-8424
1091-6490