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

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...

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Main Authors: Maske, C, Hollinshead, MS, Higbee, N, Bergo, M, Young, S, Vaux, D
Format: Journal article
Language:English
Published: 2003
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author Maske, C
Hollinshead, MS
Higbee, N
Bergo, M
Young, S
Vaux, D
author_facet Maske, C
Hollinshead, MS
Higbee, N
Bergo, M
Young, S
Vaux, D
author_sort Maske, C
collection OXFORD
description 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 nuclear lamina. Deficiency in the endoproteolysis or methylation of lamin B1 results in loss of integrity and deformity of the nuclear lamina. These data show that the organization of the nuclear envelope and lamina is dependent on a mechanism involving the methylation of lamin B1, and they identify a potential mechanism of laminopathy involving a B-type lamin.
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spelling oxford-uuid:3b68a943-fbf6-4d66-a29c-750b172d65c02022-03-26T14:07:34ZA carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3b68a943-fbf6-4d66-a29c-750b172d65c0EnglishSymplectic Elements at Oxford2003Maske, CHollinshead, MSHigbee, NBergo, MYoung, SVaux, DThe 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 nuclear lamina. Deficiency in the endoproteolysis or methylation of lamin B1 results in loss of integrity and deformity of the nuclear lamina. These data show that the organization of the nuclear envelope and lamina is dependent on a mechanism involving the methylation of lamin B1, and they identify a potential mechanism of laminopathy involving a B-type lamin.
spellingShingle Maske, C
Hollinshead, MS
Higbee, N
Bergo, M
Young, S
Vaux, D
A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.
title A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.
title_full A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.
title_fullStr A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.
title_full_unstemmed A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.
title_short A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.
title_sort carboxyl terminal interaction of lamin b1 is dependent on the caax endoprotease rce1 and carboxymethylation
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AT hollinsheadms acarboxylterminalinteractionoflaminb1isdependentonthecaaxendoproteaserce1andcarboxymethylation
AT higbeen acarboxylterminalinteractionoflaminb1isdependentonthecaaxendoproteaserce1andcarboxymethylation
AT bergom acarboxylterminalinteractionoflaminb1isdependentonthecaaxendoproteaserce1andcarboxymethylation
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AT vauxd carboxylterminalinteractionoflaminb1isdependentonthecaaxendoproteaserce1andcarboxymethylation