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Adaptor complex-independent clathrin function in yeast.

B G Yeung¹, H L Phan, G S Payne

¹Department of Biological Chemistry, School of Medicine, University of California, Los Angeles, California 90095, USA.

Molecular Biology of the Cell

|November 17, 1999

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Clathrin-associated adaptor protein (AP) complexes are not essential for clathrin function in yeast. Alternative factors likely mediate clathrin coat assembly and cargo selection in Saccharomyces cerevisiae.

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Clathrin-associated adaptor protein (AP) complexes are crucial for clathrin-coated vesicle formation.
Their roles in cargo selection and coat assembly are well-established in various model organisms.
The specific functions of AP complexes in Saccharomyces cerevisiae, particularly concerning clathrin-mediated transport, require detailed investigation.

Purpose of the Study:

To systematically characterize the subunit composition and function of AP complexes in Saccharomyces cerevisiae.
To determine the necessity of AP complexes for clathrin function, including coat assembly and cargo selection.
To identify potential alternative factors involved in clathrin-mediated vesicle formation in yeast.

Main Methods:

Related Experiment Videos

Coimmunoprecipitation assays to define AP complex subunit composition.

In vitro binding assays to assess interactions between AP complexes and clathrin.

Genetic disruption of AP subunit genes in yeast strains with wild-type and temperature-sensitive clathrin.

Gel filtration chromatography to analyze clathrin-coated vesicle profiles.

Main Results:

The subunit compositions of AP-1 and AP-2R complexes were defined, assigning all 13 yeast AP subunits to three complexes.
Only AP-1 directly interacts with clathrin, and its disruption exacerbates defects in clathrin-mutant yeast.
However, AP complex deletions showed no impact on growth, pheromone maturation, or vesicle formation in wild-type clathrin yeast, indicating dispensability.
Combined deletion of beta-subunit genes did not impair clathrin-dependent sorting in endocytic and vacuolar pathways.

Conclusions:

AP complexes are dispensable for clathrin function in Saccharomyces cerevisiae under normal physiological conditions.
Alternative cellular factors likely compensate for the absence of AP complexes in stimulating clathrin coat assembly and cargo selection.
This study highlights the adaptability of the clathrin-mediated vesicle formation machinery in yeast.