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...
Hauptverfasser: | Maske, C, Hollinshead, MS, Higbee, N, Bergo, M, Young, S, Vaux, D |
---|---|
Format: | Journal article |
Sprache: | English |
Veröffentlicht: |
2003
|
Ähnliche Einträge
-
CAAX-dependent modifications of the lamin proteins in the organization of the nuclear periphery.
von: Maske, C, et al.
Veröffentlicht: (2004) -
Ritonavir and Lopinavir Suppress RCE1 and CAAX Rab Proteins Sensitizing the Liver to Organelle Stress and Injury
von: Atousa Khalatbari, et al.
Veröffentlicht: (2020-06-01) -
Immobilisation of cocoa aspartic endoprotease
von: Shinde, S. V., et al.
Veröffentlicht: (1999) -
Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box
von: Semen M. Bondarenko, et al.
Veröffentlicht: (2020-01-01) -
Severe hepatocellular disease in mice lacking one or both CaaX prenyltransferases[S]
von: Shao H. Yang, et al.
Veröffentlicht: (2012-01-01)