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  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.

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-27EB-F Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-27EF-7
Genre: Journal Article

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Weber, K.1, Author           
Plessmann, U.1, Author           
Traub, P., Author
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1Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578618              

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 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

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Language(s): eng - English
 Dates: 1989-11-06
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0014-5793(89)81584-4
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 257 (2) Sequence Number: - Start / End Page: 411 - 414 Identifier: -