Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum
Articolo
Data di Pubblicazione:
2008
Citazione:
Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum / P. Ronchi, S. Colombo, M. Francolini, N. Borgese. - In: THE JOURNAL OF CELL BIOLOGY. - ISSN 0021-9525. - 181:1(2008 Apr 07), pp. 105-18-118. [10.1083/jcb.200710093]
Abstract:
The length and hydrophobicity of the transmembrane domain (TMD) play an important role in the sorting of membrane proteins within the secretory pathway; however, the relative contributions of protein-protein and protein-lipid interactions to this phenomenon are currently not understood. To investigate the mechanism of TMD-dependent sorting, we used the following two C tail-anchored fluorescent proteins (FPs), which differ only in TMD length: FP-17, which is anchored to the endoplasmic reticulum (ER) membrane by 17 uncharged residues, and FP-22, which is driven to the plasma membrane by its 22-residue-long TMD. Before export of FP-22, the two constructs, although freely diffusible, were seen to distribute differently between ER tubules and sheets. Analyses in temperature-blocked cells revealed that FP-17 is excluded from ER exit sites, whereas FP-22 is recruited to them, although it remains freely exchangeable with the surrounding reticulum. Thus, physicochemical features of the TMD influence sorting of membrane proteins both within the ER and at the ER-Golgi boundary by simple receptor-independent mechanisms based on partitioning.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Animals ; Membrane Glycoproteins ; Endoplasmic Reticulum ; Humans ; Recombinant Fusion Proteins ; Viral Envelope Proteins ; Membrane Proteins ; Hela Cells ; Luminescent Proteins ; Cercopithecus aethiops ; Protein Structure, Tertiary ; Cell Line ; Protein Transport
Elenco autori:
P. Ronchi, S. Colombo, M. Francolini, N. Borgese
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