A Membrane Protein Enriched in Endoplasmic Reticulum Exit Sites Interacts with COPII

Tang, Bor Luen; Ong, Yan Shan; Huang, Bing; Wei, Shichao; Wong, Ee Tsin; Qi, Robert Z.; Horstmann, Heinrich; Hong, Wanjin

doi:10.1074/jbc.m106189200

Cited by 70 publications

(72 citation statements)

References 60 publications

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“…Indeed, consistent with the biochemical data that the yeast Yip1p (Heidtman et al, 2003) and the mammalian YIP1 (Tang et al, 2001) are involved in the regulation of ER-to-Golgi traffic, human YIP1 clusters tightly with Rab1A ( Figure 2). Furthermore, YIP3/PRA1 promotes Rab dissociation from GDI during loading onto Golgi membranes (Hutt et al, 2000;Sivars et al, 2003) and has an important role in ER-to-Golgi and Golgi transport (Hutt et al, 2000;Abdul-Ghani et al, 2001).…”

Section: Rab Effectorssupporting

confidence: 72%

Large-Scale Profiling of Rab GTPase Trafficking Networks: The Membrome

Gürkan

Lapp

Alory

et al. 2005

MBoC

116

107

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Rab GTPases and SNARE fusion proteins direct cargo trafficking through the exocytic and endocytic pathways of eukaryotic cells. We have used steady state mRNA expression profiling and computational hierarchical clustering methods to generate a global overview of the distribution of Rabs, SNAREs, and coat machinery components, as well as their respective adaptors, effectors, and regulators in 79 human and 61 mouse nonredundant tissues. We now show that this systems biology approach can be used to define building blocks for membrane trafficking based on Rab-centric protein activity hubs. These Rab-regulated hubs provide a framework for an integrated coding system, the membrome network, which regulates the dynamics of the specialized membrane architecture of differentiated cells. The distribution of Rab-regulated hubs illustrates a number of facets that guides the overall organization of subcellular compartments of cells and tissues through the activity of dynamic protein interaction networks. An interactive website for exploring datasets comprising components of the Rab-regulated hubs that define the membrome of different cell and organ systems in both human and mouse is available at http://www.membrome.org/. INTRODUCTIONUnderstanding the molecular basis for the organization of the exocytic and endocytic membrane trafficking pathways in the eukaryotic cell remains a formidable challenge. The foundation of these pathways is the lipid bilayer that separates different subcellular compartments, their distinguishing features encoded by phospholipid composition, and unique sets of integral and peripheral membrane proteins. By harnessing and regulating the fundamental processes of membrane fission and fusion through the action of protein complexes, the lipid bilayer can be exploited to produce a variety of distinct subcellular compartments with unique chemical environments that play essential roles in cell and organ function. Moreover, it is now evident that these subcellular compartments are dynamic structures in continuous and specific communication through carrier vesicles and tubules that mobilize cargo to specific destinations. They can be disassembled and reassembled in a remarkably facile manner in response to cell signaling pathways, mitosis, or by simple chemical perturbants.Implicit in these dynamic pathways is the need to systematically and reversibly regulate protein interactions. Although traditional phylogenetic analyses provided significant insights into the diversity of components that direct membrane traffic (Pereira-Leal and Seabra, 2000;Chen and Scheller, 2001;Pereira-Leal and Seabra, 2001), our understanding of the basic cellular building blocks that organize this diversity into contiguous pathways is still fragmentary. Reductionist approaches using biochemical and molecular tools also provide important insights into specific steps of a pathway. However, understanding the global interconnectivities of complex biological pathways, such as cargo trafficking, will require new approaches utilizing modern ...

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Section: Rab Effectorssupporting

confidence: 72%

Large-Scale Profiling of Rab GTPase Trafficking Networks: The Membrome

Gürkan

Lapp

Alory

et al. 2005

MBoC

116

107

View full text Add to dashboard Cite

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“…It is predominantly located at the Golgi membranes, but when expressed at high levels it can also be found in the ER [30]. The mammalian homologs (Yip1 and Yip1A) are found in the Golgi and at ER exit sites [31]. Recent studies show that Yip1A regulates the membrane association of Rab6, indicating a role in the Golgi or TGN [32].…”

Section: Vesicle Tethering Components Of the Syp61 Compartmentmentioning

confidence: 99%

Isolation and proteomic analysis of the SYP61 compartment reveal its role in exocytic trafficking in Arabidopsis

et al. 2011

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The endomembrane system is a complex and dynamic intracellular trafficking network. It is very challenging to track individual vesicles and their cargos in real time; however, affinity purification allows vesicles to be isolated in their natural state so that their constituent proteins can be identified. Pioneering this approach in plants, we isolated the SYP61 trans-Golgi network compartment and carried out a comprehensive proteomic analysis of its contents with only minimal interference from other organelles. The proteome of SYP61 revealed the association of proteins of unknown function that have previously not been ascribed to this compartment. We identified a complete SYP61 SNARE complex, including regulatory proteins and validated the proteome data by showing that several of these proteins associated with SYP61 in planta. We further identified the SYP121-complex and cellulose synthases, suggesting that SYP61 plays a role in the exocytic trafficking and the transport of cell wall components to the plasma membrane. The presence of proteins of unknown function in the SYP61 proteome including ECHIDNA offers the opportunity to identify novel trafficking components and cargos. The affinity purification of plant vesicles in their natural state provides a basis for further analysis and dissection of complex endomembrane networks. The approach is widely applicable and can afford the study of several vesicle populations in plants, which can be compared with the SYP61 vesicle proteome.

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“…The mouse homolog of Yip1p, called Yip1A, is localized to ER exit sites and vesicular-tubular structures, which carry cargo to the Golgi. Evidence for a role in membrane traffic has come from the observation that the overexpression of the cytoplasmic tail of Yip1A inhibits transport of vesicular stomatitis virus envelope glycoprotein to the cell surface in normal rat kidney cells infected with vesicular stomatitis virus (35).…”

Section: A Novel Role For the Yip1p Family In Membrane Fusion-mentioning

confidence: 99%

The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

Barrowman¹,

Wang²,

Zhang

et al. 2003

Journal of Biological Chemistry

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Here we report that Yip1p and Yif1p, two members of an integral membrane protein complex that bind to the Rab Ypt1p, are required for membrane fusion with the Golgi in vitro. To block fusion, anti-Yip1p or anti-Yif1p antibodies must be added before vesicles bud from the endoplasmic reticulum (ER). These antibodies do not block the packaging of Yip1p, Yif1p, or the soluble NSF attachment protein receptor (SNAREs) into vesicles. We propose that Yip1p and Yif1p perform a critical role in establishing the fusion competence of ER to Golgi vesicles at the time of budding. Consistent with this proposal, we observe that the Yip1p⅐Yif1p complex binds to the ER to Golgi SNAREs Bos1p and Sec22p, two components of the membrane fusion machinery.

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A Membrane Protein Enriched in Endoplasmic Reticulum Exit Sites Interacts with COPII

Cited by 70 publications

References 60 publications

Large-Scale Profiling of Rab GTPase Trafficking Networks: The Membrome

Large-Scale Profiling of Rab GTPase Trafficking Networks: The Membrome

Isolation and proteomic analysis of the SYP61 compartment reveal its role in exocytic trafficking in Arabidopsis

The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

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