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PMID: 6270160 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Preferential phosphorylation of the 150,000 molecular weight component of neurofilaments by a cyclic AMP-dependent, microtubule-associated protein kinase.

The Journal of cell biology ·Vol. 90 ·No. 3 ·1981-09-00 ·Pages 755-60

Leterrier JF, Liem RK, Shelanski ML

Abstract

Highly purified preparations of bovine brain and rabbit nerve root neurofilaments were found to be lacking in protein kinase activity when either histone FIIA or the neurofilaments themselves were used as acceptors. There was no augmentation of activity in the presence of cyclic AMP. Addition of microtubule proteins prepared by cycles of assembly and disassembly resulted in phosphorylation of histone, phosphorylation of tubulin and the microtubule-associated proteins, and phosphorylation of neurofilament subunits. The phosphorylation of neurofilaments was predominantly in the 150,000-dalton species and was completely cyclic AMP dependent.

MeSH Terms
Animals Cattle Cyclic AMP/pharmacology Cytoskeleton/metabolism Microtubules/enzymology Nerve Tissue Proteins/metabolism Neurofilament Proteins Phosphorylation Protein Kinases/metabolism Rabbits Tubulin/metabolism
Chemicals
Nerve Tissue Proteins Neurofilament Proteins Tubulin Cyclic AMP Protein Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Leterrier J F
Liem R K
Shelanski M L
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28 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.90.3.755
Published
1981-09-00
Pages
755-60
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2111909
Subset
IM
Grants
NINDS NIH HHS · NS-00487 · United States
NINDS NIH HHS · NS-15076 · United States
NINDS NIH HHS · NS-15182 · United States
External Links
PubMed source DOI: 10.1083/jcb.90.3.755 PMC Full Text View journal details
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