The peroxisomal protein import machinery - a case report of transient ubiquitination with a new flavor

• Tipo: Outra Publicação em Revista Científica Internacional
• Data: 2009

Autores

grou, cp (Autor) Outra; carvalho, af (Autor) Outra; pinto, mp (Autor) Outra; alencastre, is (Autor) Outra; rodrigues, ta (Autor) Outra; freitas, mo (Autor) Outra; francisco, t (Autor) Outra; sa-miranda, c (Autor) Outra; azevedo, je (Autor) ICBAS

Revista

Título: Cellular and Molecular Life Sciences

Vol. 66

Páginas: 254-262

ISSN: 1420-682X

Editora: Springer Nature

Indexação

ISI Web of Knowledge - 25 Citações

Scopus - 28 Citações

Outras Informações

ID Authenticus: P-003-PBS

DOI: 10.1007/s00018-008-8415-5

Abstract (EN): The peroxisomal protein import machinery displays remarkable properties. Be it its capacity to accept already folded proteins as substrates, its complex architecture or its energetics, almost every aspect of this machinery seems unique. The list of unusual properties is still growing as shown by the recent finding that one of its central components, Pex5p, is transiently monoubiquitinated at a cysteine residue. However, the data gathered in recent years also suggest that the peroxisomal import machinery is not that exclusive and similarities with p97/Cdc48-mediated processes and with multisubunit RING-E3 ligases are starting to emerge. Here, we discuss these data trying to distill the principles by which this complex machinery operates.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 9