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Titolo:
mARVCF cellular localisation and binding to cadherins is influenced by thecellular context but not by alternative splicing
Autore:
Waibler, Z; Schafer, A; Starzinski-Powitz, A;
Indirizzi:
Univ Frankfurt, Inst Anthropol & Humangenet Biol, D-60054 Frankfurt, Germany Univ Frankfurt Frankfurt Germany D-60054 iol, D-60054 Frankfurt, Germany
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 21, volume: 114, anno: 2001,
pagine: 3873 - 3884
SICI:
0021-9533(200111)114:21<3873:MCLABT>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARDIO-FACIAL SYNDROME; SEGMENT POLARITY GENE; ADHESION MOLECULE UVOMORULIN; N-CADHERIN; COMPLEX-FORMATION; BETA-CATENIN; PROTEIN INTERACTIONS; CARCINOMA-CELLS; ALPHA-CATENIN; ARMADILLO;
Keywords:
p120(ctn) subfamily; MOM recruitment assay; armadillo repeat protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Starzinski-Powitz, A Univ Frankfurt, Inst Anthropol & Humangenet Biol, Siesmayerstr 70, D-60054Frankfurt, Germany Univ Frankfurt Siesmayerstr 70 Frankfurt Germany D-60054
Citazione:
Z. Waibler et al., "mARVCF cellular localisation and binding to cadherins is influenced by thecellular context but not by alternative splicing", J CELL SCI, 114(21), 2001, pp. 3873-3884

Abstract

ARVCF, a member of the catenin family, is thought to contribute to the morphoregulatory function of the cadherin-catenin complex. Recently, we reported the isolation and characterisation of murine ARVCF (mARVCF), particularly its interaction with M-cadherin. Here, we describe the identification of novel mARVCF isoforms that arise by alternative splicing. At the N-terminus, alternative splicing results in the inclusion or omission of a coiled-coil region probably important for protein-protein interactions. At the C-terminus, four isoforms also differ by domains potentially important for selective protein-protein interaction. The eight putative mARVCF isoforms were expressed as EGFP-fusion proteins in six different cell lines that exhibit a distinct pattern of cadherins. Apparently, binding of the mARVCF isoforms to M-, N-, or E-cadherin is generally unaffected by their altered N- and C-termini, as revealed by the MOM recruitment assay. However, mARVCF isoforms reproducibly exhibit differential localisation in distinct cellular environments. For example, mARVCF isoforms are unable to colocalise with N-cadherin in EJ28 carcinoma cells but do so in HeLa cells. Our results suggest thatthe subcellular localisation of mARVCF may be determined not only by the presence or absence of an appropriate interaction partner, in this case cadherins, but also by the cellular context.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 09:54:57