Journal
TRAFFIC
Volume 15, Issue 5, Pages 546-557Publisher
WILEY
DOI: 10.1111/tra.12155
Keywords
Candida albicans; endocytosis; Mid2; pheromone; polarity; pseudohyphae; Saccharomyces cerevisiae; stress
Categories
Funding
- MRC [G0601600]
- BBSRC [BB/K002511/1]
- BBSRC [BB/K002511/1, BB/J017094/1] Funding Source: UKRI
- MRC [G0601600] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K002511/1, BB/J017094/1] Funding Source: researchfish
- Medical Research Council [G0601600] Funding Source: researchfish
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The AP-2 complex is a heterotetrameric endocytic cargo-binding adaptor that facilitates uptake of membrane proteins during mammalian clathrin-mediated endocytosis. While budding yeast has clear homologues of all four AP-2 subunits which form a complex and localize to endocytic sites in vivo, the function of yeast AP-2 has remained enigmatic. Here, we demonstrate that AP-2 is required for hyphal growth in Candida albicans and polarized cell responses in Saccharomyces cerevisiae. Deletion of APM4, the cargo-binding mu subunit of AP-2, causes defects in pseudohyphal growth, generation of a mating projection and the cell wall damage response. In an apm4 null mutant, the cell wall stress sensor Mid2 is unable to relocalize to the tip of a mating projection following pheromone addition, or to the mother bud neck in response to cell wall damage. A direct binding interaction between Mid2 and the mu homology domain of Apm4 further supports a model in which AP-2 binds Mid2 to facilitate its internalization and relocalization in response to specific signals. Thus, Mid2 is the first cargo for AP-2 identified in yeast. We propose that endocytic recycling of Mid2 and other components is required for polarized cell responses ensuring cell wall deposition and is tightly monitored during cell growth.
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