Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations.

Elrod-Erickson, Matthew; Kaiser, Chris A.

doi:10.1091/mbc.7.7.1043

Cited by 152 publications

(170 citation statements)

References 48 publications

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“…Deletion of EMP24 or ERV25 suppresses the sec13-1 temperature-sensitive mutation and even bypasses a complete deletion of SEC13 (7). As an additional test of function, we found that the ⌬24-EME mutation did not suppress sec13-1 as ex- FIG.…”

Section: Coat Binding Properties Of the Emp24p And Erv25pmentioning

confidence: 77%

“…Previous studies showed that deletion of EMP24 bypassed the requirement for SEC13 (7). Therefore, we crossed the sec13-1 mutation into our strains and scored for growth at 37°C.…”

Section: Resultsmentioning

confidence: 99%

“…A recent report indicates that binding of Sec13p-Sec31p stimulates the Sec23p-Sec24p GAP activity toward Sar1p (36), therefore the recruitment of Sec13p-Sec31p by p24 proteins could influence the rate of GTP hydrolysis by Sar1p. Such a regulatory role may also explain how deletions of Emp24p or Erv25p bypass loss of function mutations in the Sec13p subunit of COPII (7).…”

Section: Coat Binding Properties Of the Emp24p And Erv25pmentioning

confidence: 99%

“…invertase and the GPI-anchored protein Gas1p), while ER resident proteins that contain an HDEL retrieval motif are secreted and the unfolded protein response pathway is activated (6 -9). Based on these and other findings, the p24 proteins have been proposed to act as structural components of vesicles (10), as cargo receptors (11), as negative regulators of vesicle budding (7) or to establish specialized subdomains on organellar membranes (12,13). There are eight p24 proteins in yeast encoded by EMP24, ERV25, and ERP1-ERP6 (14).…”

mentioning

confidence: 98%

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Distinct Roles for the Cytoplasmic Tail Sequences of Emp24p and Erv25p in Transport between the Endoplasmic Reticulum and Golgi Complex

Belden

Barlowe

2001

Journal of Biological Chemistry

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Heteromeric complexes of p24 proteins cycle between early compartments of the secretory pathway and are required for efficient protein sorting. Here we investigated the role of cytoplasmically exposed tail sequences on two p24 proteins, Emp24p and Erv25p, in directing their movement and subcellular location in yeast. Studies on a series of deletion and chimeric Emp24p-Erv25p proteins indicated that the tail sequences impart distinct functional properties that were partially redundant but not entirely interchangeable. Export of an Emp24p-Erv25p complex from the endoplasmic reticulum (ER) did not depend on two other associated p24 proteins, Erp1 and Erp2p. To examine interactions between the Emp24p and Erv25p tail sequences with the COPI and COPII coat proteins, binding experiments with immobilized tail peptides and coat proteins were performed. The Emp24p and Erv25p tail sequences bound the Sec13p/Sec31p subunit of the COPII coat (K d ϳ100 M), and binding depended on a pair of aromatic residues found in both tail sequences. COPI subunits also bound to these Emp24p and Erv25p peptides; however, the Erv25p tail sequence, which contains a dilysine motif, bound COPI more efficiently. These results suggest that both the Emp24p and Erv25p cytoplasmic sequences contain a di-aromatic motif that binds subunits of the COPII coat and promotes export from the ER. The Erv25p tail sequence binds COPI and is responsible for returning this complex to the ER.The secretory pathway in eukaryotic cells consists of a series of membrane-bound compartments that modify, sort and transport secretory cargo. Transport through this pathway depends on coat protein complexes that form vesicles and select specific cargo molecules for incorporation into vesicles. Current models suggest that transport between organelles is bi-directional, such that organellar constituents are recycled as secretory cargo advances. With regard to transport through the early secretory pathway, coat protein complex II (COPII) 1 catalyzes anterograde transport between the ER and Golgi whereas coat protein complex I (COPI) acts in retrograde traffic between these compartments (1). In addition to coat-dependent export of secretory cargo from the ER, retrieval (2) and retention (3) mechanisms operate to maintain overall compartmental organization.A related group of integral membrane proteins, referred to as the p24 family, are thought to act in concert with COPI and COPII to sort proteins during transport through the early secretory pathway. Initially identified on ER membranes (4) and subsequently detected as abundant proteins on COPI-and COPII-coated vesicles (5, 6), the function of p24 proteins in sorting remains unclear. In yeast strains lacking certain p24 members, some secretory proteins accumulate in the ER (e.g. invertase and the GPI-anchored protein Gas1p), while ER resident proteins that contain an HDEL retrieval motif are secreted and the unfolded protein response pathway is activated (6 -9). Based on these and other findings, the p24 proteins have been propo...

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Section: Coat Binding Properties Of the Emp24p And Erv25pmentioning

confidence: 77%

“…Previous studies showed that deletion of EMP24 bypassed the requirement for SEC13 (7). Therefore, we crossed the sec13-1 mutation into our strains and scored for growth at 37°C.…”

Section: Resultsmentioning

confidence: 99%

Section: Coat Binding Properties Of the Emp24p And Erv25pmentioning

confidence: 99%

mentioning

confidence: 98%

See 2 more Smart Citations

Distinct Roles for the Cytoplasmic Tail Sequences of Emp24p and Erv25p in Transport between the Endoplasmic Reticulum and Golgi Complex

Belden

Barlowe

2001

Journal of Biological Chemistry

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“…Emp24p, a member of this family, is necessary for efficient packaging of Gas1p into ER-derived vesicles and can be directly cross-linked to Gas1p (61). EMP24 was also identified as a BST2 gene that bypasses the requirement for Sec13p in coat protein complex II (COPII) vesicle formation (62). Recently it was reported that BST1, which also bypasses sec13 mutant, encodes a functional yeast homologue of mammalian GPI inositol deacylase (63).…”

Section: Roles Of Multicopy Suppressors In Gpi7mentioning

confidence: 99%

GPI7 Involved in Glycosylphosphatidylinositol Biosynthesis Is Essential for Yeast Cell Separation

Fujita

Yoko-o

Okamoto

et al. 2004

Journal of Biological Chemistry

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GPI7 is involved in adding ethanolaminephosphate to the second mannose in the biosynthesis of glycosylphosphatidylinositol (GPI) in Saccharomyces cerevisiae. We isolated gpi7 mutants, which have defects in cell separation and a daughter cell-specific growth defect at the non-permissive temperature. WSC1, RHO2, ROM2, GFA1, and CDC5 genes were isolated as multicopy suppressors of gpi7-2 mutant. Multicopy suppressors could suppress the growth defect of gpi7 mutants but not the cell separation defect. Loss of function mutations of genes involved in the Cbk1p-Ace2p pathway, which activates the expression of daughter-specific genes for cell separation after cytokinesis, bypassed the temperaturesensitive growth defect of gpi7 mutants. Furthermore, deletion of EGT2, one of the genes controlled by Ace2p and encoding a GPI-anchored protein required for cell separation, ameliorated the temperature sensitivity of the gpi7 mutant. In this mutant, Egt2p was displaced from the septal region to the cell cortex, indicating that GPI7 plays an important role in cell separation via the GPI-based modification of daughter-specific proteins in S. cerevisiae.

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Drosophila melanogasterp24 genes have developmental, tissue‐specific, and sex‐specific expression patterns and functions

Boltz

Ellis

Carney

2006

Developmental Dynamics

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Genes encoding members of the p24 family of intracellular trafficking proteins are present throughout animal and plant lineages. However, very little is known about p24 developmental, spatial, or sex-specific expression patterns or how localized expression affects function. We investigated these problems in Drosophila melanogaster, which contains nine genes encoding p24 proteins. One of these genes, logjam (loj), is expressed in the adult female nervous system and ovaries and is essential for oviposition. Nervous system-specific expression of loj, but not ovary-specific expression, rescues the behavioral defect of mutants. The Loj protein localizes to punctate structures in the cellular cytoplasm. These structures colocalize with a marker specific to the intermediate compartment and cis-Golgi, consistent with experimental evidence from other systems suggesting that p24 proteins function in intracellular transport between the endoplasmic reticulum and Golgi. Our findings reveal that Drosophila p24 transcripts are developmentally and tissue-specifically expressed. CG31787 is male-specifically expressed gene that is present during the larval, pupal, and adult stages. Female CG9053 mRNA is limited to the head, whereas males express this gene widely. Together, our studies provide experimental evidence indicating that some p24 genes have sex-specific expression patterns and tissue-and sex-limited functions. Developmental Dynamics 236:544 -555, 2007.

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Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations.

Cited by 152 publications

References 48 publications

Distinct Roles for the Cytoplasmic Tail Sequences of Emp24p and Erv25p in Transport between the Endoplasmic Reticulum and Golgi Complex

Distinct Roles for the Cytoplasmic Tail Sequences of Emp24p and Erv25p in Transport between the Endoplasmic Reticulum and Golgi Complex

GPI7 Involved in Glycosylphosphatidylinositol Biosynthesis Is Essential for Yeast Cell Separation

Drosophila melanogasterp24 genes have developmental, tissue‐specific, and sex‐specific expression patterns and functions

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