An essential but insufficient step for apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) in epithelial cells is their association with detergent-resistant microdomains (DRMs) or rafts. In this paper, we show that in MDCK cells both apical and basolateral GPI-APs associate with DRMs during their biosynthesis. However, only apical and not basolateral GPI-APs are able to oligomerize into high molecular weight complexes. Protein oligomerization begins in the medial Golgi, concomitantly with DRM association, and is dependent on protein-protein interactions. Impairment of oligomerization leads to protein missorting. We propose that oligomerization stabilizes GPI-APs into rafts and that this additional step is required for apical sorting of GPI-APs. Two alternative apical sorting models are presented.

Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins / Paladino, Simona; Sarnataro, Daniela; Pillich, R; Tivodar, S; Nitsch, Lucio; Zurzolo, Chiara. - In: THE JOURNAL OF CELL BIOLOGY. - ISSN 0021-9525. - STAMPA. - 167:4(2004), pp. 699-709. [10.1083/jcb.200407094]

Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins.

PALADINO, SIMONA;SARNATARO, DANIELA;NITSCH, LUCIO;ZURZOLO, CHIARA
2004

Abstract

An essential but insufficient step for apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) in epithelial cells is their association with detergent-resistant microdomains (DRMs) or rafts. In this paper, we show that in MDCK cells both apical and basolateral GPI-APs associate with DRMs during their biosynthesis. However, only apical and not basolateral GPI-APs are able to oligomerize into high molecular weight complexes. Protein oligomerization begins in the medial Golgi, concomitantly with DRM association, and is dependent on protein-protein interactions. Impairment of oligomerization leads to protein missorting. We propose that oligomerization stabilizes GPI-APs into rafts and that this additional step is required for apical sorting of GPI-APs. Two alternative apical sorting models are presented.
2004
Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins / Paladino, Simona; Sarnataro, Daniela; Pillich, R; Tivodar, S; Nitsch, Lucio; Zurzolo, Chiara. - In: THE JOURNAL OF CELL BIOLOGY. - ISSN 0021-9525. - STAMPA. - 167:4(2004), pp. 699-709. [10.1083/jcb.200407094]
File in questo prodotto:
File Dimensione Formato  
Paladino04.pdf

non disponibili

Tipologia: Documento in Post-print
Licenza: Accesso privato/ristretto
Dimensione 2.45 MB
Formato Adobe PDF
2.45 MB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/203334
Citazioni
  • ???jsp.display-item.citation.pmc??? 87
  • Scopus 203
  • ???jsp.display-item.citation.isi??? 194
social impact