Book chapter
Posttranslational Processing of Nuclear Lamins
The Enzymes, pp.21-41
Enzymes, Elsevier
01/01/2011
DOI: 10.1016/B978-0-12-381339-8.00003-2
Abstract
The nuclear lamina, a meshwork formed from intermediate filament proteins, provides a structural scaffolding for the cell nucleus. The principal proteins of the nuclear lamina are lamin A, lamin B1, lamin B2, and lamin C. Prelamin A (the precursor to mature lamin A), lamin B1, and lamin B2 contain a carboxyl-terminal CaaX motif that triggers farnesylation and methylation of a carboxyl-terminal cysteine. Prelamin A undergoes one additional processing step: the last 15 amino acids of the protein, including the farnesylcysteine methyl ester, are clipped off, releasing mature lamin A. Here, we review the posttranslational processing of the nuclear lamins and discuss its importance to health and disease.
Details
- Title: Subtitle
- Posttranslational Processing of Nuclear Lamins
- Creators
- Brandon S. J. Davies - University of California, Los AngelesCatherine Coffinier - University of California, Los AngelesShao H. Yang - University of California, Los AngelesHea-Jin Jung - University of California, Los AngelesLoren G. Fong - University of California, Los AngelesStephen G. Young - University of California System
- Contributors
- F Tamanoi (Editor)C A Hrycyna (Editor)M O Bergo (Editor)
- Resource Type
- Book chapter
- Publication Details
- The Enzymes, pp.21-41
- Publisher
- Elsevier; AMSTERDAM
- Series
- Enzymes
- DOI
- 10.1016/B978-0-12-381339-8.00003-2
- eISSN
- 1874-6047
- ISSN
- 1874-6047
- Number of pages
- 21
- Language
- English
- Date published
- 01/01/2011
- Academic Unit
- Fraternal Order of Eagles Diabetes Research Center; Biochemistry and Molecular Biology
- Record Identifier
- 9984293072702771
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