English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina.

MPS-Authors
/persons/resource/persons15998

Weber,  K.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15649

Plessmann,  U.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

2376525.pdf
(Publisher version), 453KB

Supplementary Material (public)
There is no public supplementary material available
Citation

Weber, K., Plessmann, U., & Traub, P. (1989). Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina. FEBS Letters, 257(2), 411-414. doi:10.1016/0014-5793(89)81584-4.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-27EB-F
Abstract
Lamin A, a nuclear lamina protein of differentiated cells, is synthesized as a precursor of the mature molecule. Protein sequencing of the carboxyterminal 14 kDa fragment shows a lack of the last 18 residues predicted by cDNA sequencing. The carboxy-terminal proteolytic maturation explains previous biochemical results including the loss of the polyisoprenylation site now located to the CXXM motif at the end of the chain. This view and earlier results on lamin B predict multiple post-translational modifications shared by lamins A and B. While retained by lamin B, which is present in all cells, they are lost by maturation from lamin A