A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.

Journal article

The mammalian nuclear lamina protein lamin B1 is posttranslationally modified by farnesylation, endoproteolysis, and carboxymethylation at a carboxyl-terminal CAAX motif. In this work, we demonstrate that the CAAX endoprotease Rce1 is required for lamin B1 endoproteolysis, demonstrate an independent pool of proteolyzed but nonmethylated lamin B1, as well as fully processed lamin B1, in interphase nuclei, and show a role for methylation in the organization of lamin B1 into domains of the nucle...

Expand abstract

Authors: Maske, C; Hollinshead, MS; Higbee, N; Bergo, M; Young, S

• Publication status: Published
• Journal: Journal of cell biology
• Volume: 162
• Issue: 7
• Pages: 1223-1232
• Publication date: 2003-09-01
• DOI: 10.1083/jcb.200303113
• EISSN: 1540-8140
• ISSN: 0021-9525
• Language: English
• Keywords: Mice, Inbred BALB C; Nuclear Envelope; Humans; Hela Cells; Antibodies, Monoclonal; Methylation; Endopeptidases; Interphase; Mice; Mitosis; Lamin Type B; Animals