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Titolo:
THE UNC-14 PROTEIN REQUIRED FOR AXONAL ELONGATION AND GUIDANCE IN CAENORHABDITIS-ELEGANS INTERACTS WITH THE SERINE THREONINE KINASE UNC-51/
Autore:
OGURA K; SHIRAKAWA M; BARNES TM; HEKIMI S; OHSHIMA Y;
Indirizzi:
KYUSHU UNIV,FAC SCI,DEPT BIOL FUKUOKA 81281 JAPAN KYUSHU UNIV,FAC SCI,DEPT BIOL FUKUOKA 81281 JAPAN MCGILL UNIV,DEPT BIOL MONTREAL PQ H3A 1B1 CANADA
Titolo Testata:
Genes & development
fascicolo: 14, volume: 11, anno: 1997,
pagine: 1801 - 1811
SICI:
0890-9369(1997)11:14<1801:TUPRFA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
TEMPERATURE-SENSITIVE MUTANT; C-ELEGANS; GENE-EXPRESSION; DROSOPHILA-MELANOGASTER; REVERSIBLE BLOCKAGE; ESCHERICHIA-COLI; GUIDES CELL; MIGRATIONS; ENCODES; SYSTEM;
Keywords:
C-ELEGANS; UNC-14; UNC-51; AXONAL ELONGATION; AXONAL GUIDANCE; SERINE/THREONINE KINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
K. Ogura et al., "THE UNC-14 PROTEIN REQUIRED FOR AXONAL ELONGATION AND GUIDANCE IN CAENORHABDITIS-ELEGANS INTERACTS WITH THE SERINE THREONINE KINASE UNC-51/", Genes & development, 11(14), 1997, pp. 1801-1811

Abstract

Certain une mutants in the nematode Caenorhabditis elegans, such as unc-14 and unc-51, show abnormal axonal elongation and axonal structures. We cloned the unc-51 gene previously and predicted that it encodes a novel serine/threonine protein kinase. In this study, we precisely localized the activity to rescue an unc-14 mutation. Also, we identified four cDNA clones encoded by the unc-14 rescuing region, in screens for proteins that bind to UNC-51 using a yeast two-hybrid system. A mutation site in the cDNA was identified for each of the six unc-14 mutants, establishing that the unc-14 gene was cloned. The unc-14 gene encodes a novel protein of 665 amino acids, and is coexpressed with the unc-51 gene in the cell bodies and axons of almost all neurons includingDD/VD and hermaphrodite-specific neurons. Another clone recovered in the two-hybrid screen encodes a carboxy-terminal region of UNC-51. Analysis using the yeast two-hybrid system suggested that a central region of UNC-14 bound to a carboxy-terminal region of UNC-51, and that theUNC-51 carboxy-terminal region oligomerized. In in vitro binding studies using recombinant fusion proteins, UNC-14 interacted with UNC-51 directly. We propose that UNC-51 protein kinase acts as an oligomer, and that UNC-14 is a regulator of UNC-51, in axonal elongation and guidance.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 20:11:29