Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides
نویسندگان
چکیده
منابع مشابه
Autophagic degradation of farnesylated prelamin A as a therapeutic approach to lamin-linked progeria
Farnesylated prelamin A is a processing intermediate produced in the lamin A maturation pathway. Accumulation of a truncated farnesylated prelamin A form, called progerin, is a hallmark of the severe premature ageing syndrome, Hutchinson-Gilford progeria. Progerin elicits toxic effects in cells, leading to chromatin damage and cellular senescence and ultimately causes skin and endothelial defec...
متن کاملErratum - Autophagic Degradation of Farnesylated Prelamin a as a Therapeutic Approach to Lamin-Linked Progeria
V. Cenni,1 C. Capanni,1 M. Columbaro,2 M. Ortolani,1 M.R. D’Apice,3 G. Novelli,4 M. Fini,5 S. Marmiroli,6 E. Scarano,7 N.M. Maraldi,2 S. Squarzoni,1 S. Prencipe,5 G. Lattanzi1 1National Research Council of Italy, Institute for Molecular Genetics, IGM-CNR, Unit of Bologna c/o IOR, Bologna 2Laboratory of Musculoskeletal Cell Biology, Rizzoli Orthopedic Institute, Bologna 3Department of Biopatholo...
متن کاملCOOH-terminal methylation of lamin B and inhibition of methylation by farnesylated peptides corresponding to lamin B and other CAAX motif proteins.
Previous reports from this laboratory have demonstrated that lamin B is reversibly methylesterified in a cell cycle-dependent manner. The site of this methylation, however, was not identified. In this report, we describe a single major methylated product obtained following reversed-phase high-performance liquid chromatographic analysis of peptides generated by proteolytic digestion of lamin B f...
متن کاملHuman lamin B contains a farnesylated cysteine residue.
We recently showed that HeLa cell lamin B is modified by a mevalonic acid derivative. Here we identified the modified amino acid, determined its mode of linkage to the mevalonic acid derivative, and established the derivative's structure. A cysteine residue is modified because experiments with lamin B that had been biosynthetically labeled with [3H]mevalonic acid or [35S]cysteine and then exten...
متن کاملStructural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin.
Activation of glutamate decarboxylase (GAD) by calcium-bound calmodulin (CaM) is required for normal plant growth through regulation of gamma-aminobutyrate and glutamate metabolism. The interaction of CaM with the C-terminal domain of GAD is believed to induce dimerization of the enzyme, an event implicated for Ca(2+)-dependent enzyme activation. Here, we present the solution structure of CaM i...
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ژورنال
عنوان ژورنال: Cells
سال: 2018
ISSN: 2073-4409
DOI: 10.3390/cells7040033