A Systematic Approach to Pair Secretory Cargo Receptors with Their Cargo Suggests a Mechanism for Cargo Selection by Erv14

Herzig, Yonatan; Sharpe, Hayley J.; Elbaz, Yael; Munro, Sean; Schuldiner, Maya

doi:10.1371/journal.pbio.1001329

Cited by 99 publications

(151 citation statements)

References 57 publications

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“…Finally, interactions with unidentified cargo receptors that could recognize TMDs by their length and exoplasmic volume, similar to what has been described for the ER cargo receptor Erv14 (Herzig et al, 2012), could also lead to loading of Golgi proteins into COPI vesicles.…”

Section: Features Of the Exoplasmic Hemi-tmds Define Golgi Or Plasma mentioning

confidence: 64%

Short length transmembrane domains having voluminous exoplasmic halves determine retention of Type II membrane proteins in the Golgi complex

Quiroga¹,

Trenchi²,

Montoro³

et al. 2013

Journal of Cell Science

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SummaryIt is still unclear why some proteins that travel along the secretory pathway are retained in the Golgi complex whereas others make their way to the plasma membrane. Recent bioinformatic analyses on a large number of single-spanning membrane proteins support the hypothesis that specific features of the transmembrane domain (TMD) are relevant to the sorting of these proteins to particular organelles. Here we experimentally test this hypothesis for Golgi and plasma membrane proteins. Using the Golgi SNARE protein Sft1 and the plasma membrane SNARE protein Sso1 from Saccharomyces cerevisiae as model proteins, we modified the length of their TMDs and the volume of their exoplasmic hemi-TMD, and determined their subcellular localization both in yeast and mammalian cells. We found that short TMDs with high-volume exoplasmic hemi-TMDs confer Golgi membrane residence, whereas TMDs with lowvolume exoplasmic hemi-TMDs, either short or long, confer plasma membrane residence to these proteins. Results indicate that the shape of the exoplasmic hemi-TMD, in addition to the length of the entire TMD, determine retention in the Golgi or exit to the plasma membrane of Type II membrane proteins.

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Section: Features Of the Exoplasmic Hemi-tmds Define Golgi Or Plasma mentioning

confidence: 64%

Short length transmembrane domains having voluminous exoplasmic halves determine retention of Type II membrane proteins in the Golgi complex

Quiroga¹,

Trenchi²,

Montoro³

et al. 2013

Journal of Cell Science

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“…The final hit, Erv14, posed a conundrum. As a cargo receptor, Erv14 is known to facilitate ER exit of more than 20 cargo proteins that are membrane proteins with a long transmembrane domain (TMD) (Herzig et al, 2012;Pagant et al, 2015;Powers and Barlowe, 2002). However, in contrast to the role of Erv14 in facilitating client cargos for ER exit, BMV 1a remains in ER membranes without evidence suggesting its exit from the ER (Schwartz et al, 2002).…”

Section: Resultsmentioning

confidence: 99%

“…Sec24 serves as the principle cargo recruiter by recognizing sorting signals present in cargos and recruiting them into vesicles. However, many cargos do not have Sec24-binding motifs and, therefore, require a cargo receptor to facilitate their incorporation into vesicles (Belden and Barlowe, 2001;Herzig et al, 2012;Kuehn et al, 1998;Miller et al, 2003;Mossessova et al, 2003;Pagant et al, 2015). As a typical cargo receptor, ER-vesicle protein of 14 kD (Erv14) binds to both its client cargos and Sec24 to facilitate cargo incorporation into vesicles for ER exit (Herzig et al, 2012;Pagant et al, 2015;Powers and Barlowe, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…However, many cargos do not have Sec24-binding motifs and, therefore, require a cargo receptor to facilitate their incorporation into vesicles (Belden and Barlowe, 2001;Herzig et al, 2012;Kuehn et al, 1998;Miller et al, 2003;Mossessova et al, 2003;Pagant et al, 2015). As a typical cargo receptor, ER-vesicle protein of 14 kD (Erv14) binds to both its client cargos and Sec24 to facilitate cargo incorporation into vesicles for ER exit (Herzig et al, 2012;Pagant et al, 2015;Powers and Barlowe, 2002). It has only recently been shown that COPII coat components have additional functions such as contributing to the biogenesis of autophagosomes (Davis and Ferro-Novick, 2015;Ge et al, 2014;Wang et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

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An unrecognized function for COPII components in recruiting the viral replication protein BMV 1a to the perinuclear ER

Fuchs

Zhang

et al. 2016

Journal of Cell Science

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Positive-strand RNA viruses invariably assemble their viral replication complexes (VRCs) by remodeling host intracellular membranes. How viral replication proteins are targeted to specific organelle membranes to initiate VRC assembly remains elusive. Brome mosaic virus (BMV), whose replication can be recapitulated in Saccharomyces cerevisiae, assembles its VRCs by invaginating the outer perinuclear endoplasmic reticulum (ER) membrane. Remarkably, BMV replication protein 1a (BMV 1a) is the only viral protein required for such membrane remodeling. We show that ER-vesicle protein of 14 kD (Erv14), a cargo receptor of coat protein complex II (COPII), interacts with BMV 1a. Moreover, the perinuclear ER localization of BMV 1a is disrupted in cells lacking ERV14 or expressing dysfunctional COPII coat components (Sec13, Sec24 or Sec31). The requirement of Erv14 for the localization of BMV 1a is bypassed by addition of a Sec24-recognizable sorting signal to BMV 1a or by overexpressing Sec24, suggesting a coordinated effort by both Erv14 and Sec24 for the proper localization of BMV 1a. The COPII pathway is well known for being involved in protein secretion; our data suggest that a subset of COPII coat proteins have an unrecognized role in targeting proteins to the perinuclear ER membrane.

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“…Other receptors function to enrich vesicles with membrane protein cargoes. The p24 proteins, Emp24, Erv25, Erp1, and Erp2, are required for efficient ER export of GPI-anchored proteins, whose lumenal orientation precludes direct coupling to the COPII coat (Belden and Barlowe 1996;Muniz et al 2000; Herzig et al 2012), mediate efficient export of transmembrane proteins that have cytoplasmically oriented regions but either do not contain ER export signals or require additional affinity or organization to achieve efficient capture. The requirement for receptors for such transmembrane cargoes remains unexplained, but may derive from the ancestral history of the cargoes whereby previously soluble proteins became membrane anchored as a result of gene fusion events (Dancourt and Barlowe 2010).…”

Section: Transport From the Er: Sculpting And Populating A Copii Vesiclementioning

confidence: 99%

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

2013

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The secretory pathway is responsible for the synthesis, folding, and delivery of a diverse array of cellular proteins. Secretory protein synthesis begins in the endoplasmic reticulum (ER), which is charged with the tasks of correctly integrating nascent proteins and ensuring correct post-translational modification and folding. Once ready for forward traffic, proteins are captured into ER-derived transport vesicles that form through the action of the COPII coat. COPII-coated vesicles are delivered to the early Golgi via distinct tethering and fusion machineries. Escaped ER residents and other cycling transport machinery components are returned to the ER via COPI-coated vesicles, which undergo similar tethering and fusion reactions. Ultimately, organelle structure, function, and cell homeostasis are maintained by modulating protein and lipid flux through the early secretory pathway. In the last decade, structural and mechanistic studies have added greatly to the strong foundation of yeast genetics on which this field was built. Here we discuss the key players that mediate secretory protein biogenesis and trafficking, highlighting recent advances that have deepened our understanding of the complexity of this conserved and essential process. TABLE OF CONTENTS Abstract 383Introduction 384

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A Systematic Approach to Pair Secretory Cargo Receptors with Their Cargo Suggests a Mechanism for Cargo Selection by Erv14

Abstract: A systematic approach to visualize proteins exiting the endoplasmic reticulum paired with their cargo receptors identifies novel cargo for known receptors and reveals the mechanism of one conserved receptor, Erv14.

Cited by 99 publications

References 57 publications

Short length transmembrane domains having voluminous exoplasmic halves determine retention of Type II membrane proteins in the Golgi complex

Short length transmembrane domains having voluminous exoplasmic halves determine retention of Type II membrane proteins in the Golgi complex

An unrecognized function for COPII components in recruiting the viral replication protein BMV 1a to the perinuclear ER

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

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