scholarly journals Plasma membrane protein trafficking in plant-microbe interactions: a plant cell point of view

2014 ◽  
Vol 5 ◽  
Author(s):  
Nathalie Leborgne-Castel ◽  
Karim Bouhidel
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Plant Cell ◽  
Protein Trafficking ◽  
Point Of View ◽  
Plasma Membrane Protein ◽  
Membrane Protein Trafficking ◽  
Microbe Interactions

scholarly journals BEX5/RabA1b Regulates trans-Golgi Network-to-Plasma Membrane Protein Trafficking in Arabidopsis

2012 ◽  
Vol 24 (7) ◽  
pp. 3074-3086 ◽  
Author(s):  
Elena Feraru ◽  
Mugurel I. Feraru ◽  
Rin Asaoka ◽  
Tomasz Paciorek ◽  
Riet De Rycke ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Protein Trafficking ◽  
Plasma Membrane Protein ◽  
Trans Golgi Network ◽  
Membrane Protein Trafficking ◽  
Golgi Network

scholarly journals Uni-directional ciliary membrane protein trafficking by a cytoplasmic retrograde IFT motor and ciliary ectosome shedding

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Muqing Cao ◽  
Jue Ning ◽  
Carmen I Hernandez-Lara ◽  
Olivier Belzile ◽  
Qian Wang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Protein Trafficking ◽  
Protein Composition ◽  
Cytoplasmic Dynein ◽  
Cytoplasmic Microtubule ◽  
Dynamic Regulation ◽  
Ciliary Membrane ◽  
Membrane Protein Trafficking

The role of the primary cilium in key signaling pathways depends on dynamic regulation of ciliary membrane protein composition, yet we know little about the motors or membrane events that regulate ciliary membrane protein trafficking in existing organelles. Recently, we showed that cilium-generated signaling in Chlamydomonas induced rapid, anterograde IFT-independent, cytoplasmic microtubule-dependent redistribution of the membrane polypeptide, SAG1-C65, from the plasma membrane to the periciliary region and the ciliary membrane. Here, we report that the retrograde IFT motor, cytoplasmic dynein 1b, is required in the cytoplasm for this rapid redistribution. Furthermore, signaling-induced trafficking of SAG1-C65 into cilia is unidirectional and the entire complement of cellular SAG1-C65 is shed during signaling and can be recovered in the form of ciliary ectosomes that retain signal-inducing activity. Thus, during signaling, cells regulate ciliary membrane protein composition through cytoplasmic action of the retrograde IFT motor and shedding of ciliary ectosomes.

Versatile role of the yeast ubiquitin ligase Rsp5p in intracellular trafficking

2008 ◽  
Vol 36 (5) ◽  
pp. 791-796 ◽  
Author(s):  
Naima Belgareh-Touzé ◽  
Sébastien Léon ◽  
Zoi Erpapazoglou ◽  
Marta Stawiecka-Mirota ◽  
Danièle Urban-Grimal ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Ubiquitin Ligase ◽  
Protein Trafficking ◽  
Adaptor Proteins ◽  
Binding Domains ◽  
Independent Functions ◽  
Membrane Protein Trafficking ◽  
Ubiquitin Ligase E3

The ubiquitin ligase (E3) Rsp5p is the only member of the Nedd (neural-precursor-cell-expressed, developmentally down-regulated) 4 family of E3s present in yeast. Rsp5p has several proteasome-independent functions in membrane protein trafficking, including a role in the ubiquitination of most plasma membrane proteins, leading to their endocytosis. Rsp5p is also required for the ubiquitination of endosomal proteins, leading to their sorting to the internal vesicles of MVBs (multivesicular bodies). Rsp5p catalyses the attachment of non-conventional ubiquitin chains, linked through ubiquitin Lys-63, to some endocytic and MVB cargoes. This modification appears to be required for efficient sorting, possibly because these chains have a greater affinity for the ubiquitin-binding domains present within endocytic or MVB sorting complexes. The mechanisms involved in the recognition of plasma membrane and MVB substrates by Rsp5p remain unclear. A subset of Rsp5/Nedd4 substrates have a ‘PY motif’ and are recognized directly by the WW (Trp-Trp) domains of Rsp5p. Most Rsp5p substrates do not carry PY motifs, but some may depend on PY-containing proteins for their ubiquitination by Rsp5p, consistent with the latter's acting as specificity factors or adaptors. As in other ubiquitin-conjugating systems, these adaptors are also Rsp5p substrates and undergo ubiquitin-dependent trafficking. In the present review, we discuss recent examples illustrating the role of Rsp5p in membrane protein trafficking and providing new insights into the regulation of this E3 by adaptor proteins.

scholarly journals Endoplasmic Reticulum/Plasma Membrane Junctions Function as Membrane Protein Trafficking Hubs

2013 ◽  
Vol 104 (2) ◽  
pp. 619a
Author(s):  
Philip D. Fox ◽  
Christpher J. Haberkorn ◽  
Aubrey V. Weigel ◽  
Elizabeth J. Akin ◽  
Matthew J. Kennedy ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Trafficking

scholarly journals Vps34p differentially regulates endocytosis from the apical and basolateral domains in polarized hepatic cells

2001 ◽  
Vol 154 (6) ◽  
pp. 1197-1208 ◽  
Author(s):  
Pamela L. Tuma ◽  
Lydia K. Nyasae ◽  
Jonathan M. Backer ◽  
Ann L. Hubbard
Keyword(s):  
Plasma Membrane ◽  
Protein Trafficking ◽  
Endocytic Pathway ◽  
Apical Plasma Membrane ◽  
Specific Inhibition ◽  
Class Iii ◽  
Plasma Membrane Protein ◽  
Hepatic Cells ◽  
Early Endosomes ◽  
Membrane Protein Trafficking

Using a microinjection approach to study apical plasma membrane protein trafficking in hepatic cells, we found that specific inhibition of Vps34p, a class III phosphoinositide 3 (PI-3) kinase, nearly perfectly recapitulated the defects we reported for wortmannin-treated cells (Tuma, P.L., C.M. Finnegan, J.-H Yi, and A.L. Hubbard. 1999. J. Cell Biol. 145:1089–1102). Both wortmannin and injection of inhibitory Vps34p antibodies led to the accumulation of resident apical proteins in enlarged prelysosomes, whereas transcytosing apical proteins and recycling basolateral receptors transiently accumulated in basolateral early endosomes. To understand how the Vps34p catalytic product, PI(3)P, was differentially regulating endocytosis from the two domains, we examined the PI(3)P binding protein early endosomal antigen 1 (EEA1). We determined that EEA1 distributed to two biochemically distinct endosomal populations: basolateral early endosomes and subapical endosomes. Both contained rab5, although the latter also contained late endosomal markers but was distinct from the transcytotic intermediate, the subapical compartment. When PI(3)P was depleted, EEA1 dissociated from basolateral endosomes, whereas it remained on subapical endosomes. From these results, we conclude that PI(3)P, via EEA1, regulates early steps in endocytosis from the basolateral surface in polarized WIF-B cells. However, PI(3)P must use different machinery in its regulation of the apical endocytic pathway, since later steps are affected by Vps34p inhibition.

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