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PMID: 2834726 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Protein kinase activity associated with the nuclear lamina.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 9 ·1988-05-00 ·Pages 2994-8

Dessev G, Iovcheva C, Tasheva B, Goldman R

Abstract

A nuclear lamina-enriched fraction from Ehrlich ascites tumor cells contains a tightly bound protein kinase activity, which phosphorylates in vitro the nuclear lamins, a 52-kilodalton protein, and several unknown minor components. The enzyme(s) is thermolabile, independent of Ca2+ and cAMP, and inhibited by quercetin. After treatment with 4 M urea it remains bound to the nuclear lamina in an active state, but it is irreversibly inactivated in 6 M urea. The lamin proteins are phosphorylated on serine residues. Their two-dimensional phosphopeptide maps show multiple phosphorylation sites and a considerable similarity to the phosphopeptide maps of lamins labeled in vivo. Photoaffinity labeling experiments revealed several polypeptide fractions in the nuclear lamina fraction that are candidates for the protein kinase(s).

MeSH Terms
Animals Calcium/metabolism Cell Line Cell Nucleus/enzymology Cyclic AMP/metabolism Electrophoresis, Polyacrylamide Gel Isoelectric Focusing Lamins Molecular Weight Nuclear Proteins/metabolism Phosphorylation Protein Kinases/metabolism Quercetin/pharmacology
Chemicals
Lamins Nuclear Proteins Quercetin Cyclic AMP Protein Kinases Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Dessev G
Department of Cell Biology and Anatomy, Northwestern University Medical School, Chicago, IL 60611.
Iovcheva C
Tasheva B
Goldman R
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28 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.85.9.2994
Published
1988-05-00
Pages
2994-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC280129
Subset
IM
Grants
NCI NIH HHS · R01-CA31760-06 · United States
External Links
PubMed source DOI: 10.1073/pnas.85.9.2994 PMC Full Text View journal details
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