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Titolo:
NEW NUCLEAR FUNCTIONS FOR CALMODULIN
Autore:
AGELL N; ALIGUE R; ALEMANY V; CASTRO A; JAIME M; PUJOL MJ; RIUS E; SERRATOSA J; TAULES M; BACHS O;
Indirizzi:
UNIV BARCELONA,FAC MED,DEPT CELLULAR BIOL,CASANOVA 143 BARCELONA 08036 SPAIN UNIV BARCELONA,FAC MED,DEPT CELLULAR BIOL BARCELONA 08036 SPAIN CSIC,CTR INVEST & DESENVOLUPAMENT,DEPT PHARMACOL & TOXICOL BARCELONA SPAIN
Titolo Testata:
Cell calcium
fascicolo: 2-3, volume: 23, anno: 1998,
pagine: 115 - 121
SICI:
0143-4160(1998)23:2-3<115:NNFFC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYMERASE-ALPHA ACTIVITY; BINDING PROTEINS; RAT-LIVER; DEPENDENT KINASES; CELLS; TRANSCRIPTION; LIBRARIES; PHAGE; ANTAGONISTS; ANTIBODIES;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
N. Agell et al., "NEW NUCLEAR FUNCTIONS FOR CALMODULIN", Cell calcium, 23(2-3), 1998, pp. 115-121

Abstract

The data reported here summarize a series of results which reveal newfunctions for nuclear calmodulin (CaM). The addition of CaM inhibitors to cultures of proliferating NRK cells blocked the activity of the cyclin-dependent protein kinases 4 (cdk4) and 2 (cdk2), which are enzymes implicated in the progression of Gf and in the onset of DNA replication, respectively. CaM modulates the activity of cdk4 by regulating the nuclear location of both cdk4 and cyclin D, its associated regulatory subunit. By using CaM-affinity chromatography, we have recently identified two new nuclear CaM-binding proteins: (i) the protein La/SSB, which is an autoantigen implicated in several autoimmune diseases suchas lupus erythematosus and Sjogren's syndrome (since La/SSB participates in the process of transcription mediated by RNA polymerase ill, CaM could be involved in the regulation of this process); and (ii) the protein SAP145, a member of the spliceosome-associated proteins (SAPs) which is a subunit of the splicing factor SF3(b). This finding suggests the involvement of CaM in pre-mRNA splicing. Finally, a screening for new CaM-binding proteins in the fission yeast performed by using thephage display analysis, revealed that several nucleolar-ribosomal proteins associate to CaM, suggesting that CaM modulates ribosomal assembly and/or function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 15:36:57