2013
DOI: 10.1074/jbc.m113.518340
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Isoform-selective Oligomer Formation of Saccharomyces cerevisiae p24 Family Proteins

Abstract: Background: p24 family proteins function as cargo receptors for ER-Golgi transport. Results: Genetic and physical interactions among eight known and one newly identified S. cerevisiae p24 proteins were determined. Conclusion: Yeast p24 proteins function in several functionally redundant complexes, including one containing a novel p24 isoform induced under respiratory conditions. Significance: This is the first comprehensive study of the yeast p24 complexes.

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Cited by 18 publications
(22 citation statements)
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“…Previous study in yeast uncovered that the different p24 sub-family members form diverse complexes, thus playing multiple roles in escorting cargoes [31]. Consistent with the yeast work, we found that different p24 proteins play different roles and cannot be replaced by each other, indicating the functional diversity of the p24 family.…”
Section: Discussionsupporting
confidence: 90%
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“…Previous study in yeast uncovered that the different p24 sub-family members form diverse complexes, thus playing multiple roles in escorting cargoes [31]. Consistent with the yeast work, we found that different p24 proteins play different roles and cannot be replaced by each other, indicating the functional diversity of the p24 family.…”
Section: Discussionsupporting
confidence: 90%
“…Several p24 proteins, including Baiser, CHOp24, Eclair, Opm and p24-1 [16,17], are involved in this process. These p24 family members are functionally diverse and cannot be replaced by each other, probably function in a partially redundant manner and/or by forming diverse complexes [31]. …”
Section: Resultsmentioning
confidence: 99%
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“…The p24 proteins assemble in a heteromeric complex that cycles between the ER and Golgi compartments [16,[18][19][20][21]. Experimental evidence from yeast and mammalian cell systems suggests a specific role of the p24 complex as a transmembrane adaptor or cargo receptor that could link remodeled GPI-APs to the cytosolic COPII coat, ensuring their selective incorporation into nascent COPII vesicles [10][11][12].…”
Section: Introductionmentioning
confidence: 98%
“…1D). Redundancy among p24␣ and p24␥ proteins had been described recently in yeast (11). Because the GPI-AP transport was impaired in p24␥ 2 knockdown cells and could not be compensated by the slight overexpression of other p24␥ proteins (Fig.…”
Section: Discussionmentioning
confidence: 99%