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Titolo:
The homeodomain coordinates nuclear entry of the Lhx3 neuroendocrine transcription factor and association with the nuclear matrix
Autore:
Parker, GE; Sandoval, RM; Feister, HA; Bidwell, JP; Rhodes, SJ;
Indirizzi:
Indiana Univ Purdue Univ, Dept Biol, Indianapolis, IN 46202 USA Indiana Univ Purdue Univ Indianapolis IN USA 46202 anapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Med,Div Nephrol, Renal Epithelial Biol Expt Lab Imaging Facil, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 Facil, Indianapolis, IN 46202 USA Indiana Univ, Sch Dent, Dept Periodont, Indianapolis, IN 46202 USA IndianaUniv Indianapolis IN USA 46202 iodont, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Anat & Cell Biol, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 l Biol, Indianapolis, IN 46202 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 31, volume: 275, anno: 2000,
pagine: 23891 - 23898
SICI:
0021-9258(20000804)275:31<23891:THCNEO>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOTIC APPARATUS PROTEIN; DOMAIN INTERACTOR NLI; CLASS HOMEOBOX GENE; LOCALIZATION SIGNAL; DIFFERENTIAL ACTIVATION; LIM; EXPRESSION; PITUITARY; IDENTIFICATION; ISOFORMS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Rhodes, SJ Indiana Univ Purdue Univ, Dept Biol, 723 W Michigan St, Indianapolis, IN 46202 USA Indiana Univ Purdue Univ 723 W Michigan St IndianapolisIN USA 46202
Citazione:
G.E. Parker et al., "The homeodomain coordinates nuclear entry of the Lhx3 neuroendocrine transcription factor and association with the nuclear matrix", J BIOL CHEM, 275(31), 2000, pp. 23891-23898

Abstract

LIM homeodomain transcription factors regulate development in complex organisms. To characterize the molecular signals required for the nuclear localization of these proteins, we examined the Lhx3 factor. Lhx3 is essential for pituitary organogenesis and motor neuron specification. By using functional fluorescent derivatives, we demonstrate that Lhx3 is found in both the nucleoplasm and nuclear matrix. Three nuclear localization signals were mapped within the homeodomain, and one was located in the carboxyl terminus. The homeodomain also serves as the nuclear matrix targeting sequence. No individual signal is alone required for nuclear localization of Lhx3; the signals work in combinatorial fashion. Specific combinations of these signals transferred nuclear localization to cytoplasmic proteins. Mutation of nuclear localization signals within the homeodomain inhibited Lhx3 transcriptional function. By contrast, mutation of the carboxyl-terminal signal activatedLhx3, indicating that this region is critical to transcriptional activity and may be a target of regulatory pathways. The pattern of conservation of the nuclear localization and nuclear matrix targeting signals suggests thatthe LIM homeodomain factors use similar mechanisms for subcellular localization. Furthermore, upon nuclear entry, association of Lhx3 with the nuclear matrix may contribute to LIM homeodomain factor interaction with other classes of transcription factors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/10/20 alle ore 05:30:33