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Titolo:
PHOSPHORYLATION OF MYOSIN REGULATORY LIGHT-CHAINS BY THE MOLLUSCAN TWITCHIN KINASE
Autore:
HEIERHORST J; PROBST WC; KOHANSKI RA; BUKU A; WEISS KR;
Indirizzi:
ST VINCENTS INST MED RES,41 VICTORIA PARADE FITZROY VIC 3065 AUSTRALIA CUNY MT SINAI SCH MED,DEPT PHYSIOL & BIOPHYS NEW YORK NY 10029 CUNY MT SINAI SCH MED,DEPT BIOCHEM NEW YORK NY 10029
Titolo Testata:
European journal of biochemistry
fascicolo: 2, volume: 233, anno: 1995,
pagine: 426 - 431
SICI:
0014-2956(1995)233:2<426:POMRLB>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE MYOSIN; CAENORHABDITIS-ELEGANS; SEQUENCE-ANALYSIS; PROTEIN;
Keywords:
PROTEIN KINASE; TWITCHIN; TITIN; PROJECTIN; MYOSIN LIGHT CHAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
J. Heierhorst et al., "PHOSPHORYLATION OF MYOSIN REGULATORY LIGHT-CHAINS BY THE MOLLUSCAN TWITCHIN KINASE", European journal of biochemistry, 233(2), 1995, pp. 426-431

Abstract

The unusually large (approximate to 600 to >3000 kDa) myosin-associated proteins of the titin/twitchin superfamily are considered to be important cytoskeletal rulers for thick filament assembly in muscle. Thisfunction is maintained by approximately 60-240 modular fibronectin-type-III and immunoglobulin-C2 repeats in these proteins which further contain a protein serine/threonine kinase domain of unknown function. In this study, the bacterially expressed kinase domain of Aplysia twitchin was used in order to identify a potential physiological substrate. Addition of the recombinant kinase to Aplysia actomyosin preparationsresulted in the specific phosphorylation of the 19-kDa myosin regulatory light chains. The twitchin kinase phosphorylated purified light chains on Thr15 in a region which shared a high degree of similarity with the phosphorylation site fur vertebrate smooth muscle myosin light chain kinase. Peptide analogs of the twitchin substrate sequence and the similar sequence in vertebrate smooth muscle myosin light chains were phosphorylated with good kinetic properties. These data reveal the first potential substrate for any of the giant protein kinases and support a dual role of twitchin in molluscan muscle as a cytoskeletal protein as well as a myosin light chain kinase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 18:07:58