Estamos realizando la búsqueda. Por favor, espere...
1448
37
174
31686
4649
2689
362
417
Abstract: Retromer is a multi-protein complex that recycles transmembrane cargo from endosomes to the trans-Golgi network and the plasma membrane. Defects in retromer impair various cellular processes and underlie some forms of Alzheimer's disease and Parkinson's disease. Although retromer was discovered over 15 years ago, the mechanisms for cargo recognition and recruitment to endosomes have remained elusive. Here, we present an X-ray crystallographic analysis of a four-component complex comprising the VPS26 and VPS35 subunits of retromer, the sorting nexin SNX3, and a recycling signal from the divalent cation transporter DMT1-II. This analysis identifies a binding site for canonical recycling signals at the interface between VPS26 and SNX3. In addition, the structure highlights a network of cooperative interactions among the VPS subunits, SNX3, and cargo that couple signal-recognition to membrane recruitment
Fuente: Cell, 2016, 167(6), 1623-1635
Editorial: Elsevier (Cell Press)
Año de publicación: 2016
Nº de páginas: 28
Tipo de publicación: Artículo de Revista
DOI: 10.1016/j.cell.2016.10.056
ISSN: 0092-8674,1097-4172
Proyecto español: BFU2014-59759-R
Url de la publicación: http://dx.doi.org/10.1016/j.cell.2016.10.056
Google Scholar
Citas
Repositorio UCrea Leer publicación
MARIA JESUS LUCAS GAY
GERSHLICK, DAVID C.
VIDAURRAZAGA, ANDER
ROJAS, ADRIANA L.
BONIFACINO, JUAN S.
HIERRO, AITOR
Volver