Crystal Structure of the Epo1-Bem3 Complex for Bud Growth.
Tubules of the endoplasmic reticulum (ER) spread into the buds of yeast by an actin-based mechanism and, upon entry, become attached to the polarisome, a proteinaceous micro-compartment below the tip of the bud. The minimal tether between polarisome and cortical ER is formed by a protein complex consisting of Epo1, ... a member of the polarisome, Scs2, a membrane protein of the ER and Cdc42 guanosine triphosphatase-activating protein Bem3. Here, we report the crystal structure of a complex between Epo1 and Bem3. In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1. Our findings provide a first structural insight into the molecular architecture of the link between cortical ER and the polarisome.
Mesh Terms:
Amino Acid Sequence, Carrier Proteins, Crystallography, X-Ray, GTPase-Activating Proteins, Magnetic Resonance Spectroscopy, Models, Molecular, Multiprotein Complexes, Protein Binding, Protein Conformation, Protein Multimerization, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship
Amino Acid Sequence, Carrier Proteins, Crystallography, X-Ray, GTPase-Activating Proteins, Magnetic Resonance Spectroscopy, Models, Molecular, Multiprotein Complexes, Protein Binding, Protein Conformation, Protein Multimerization, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship
Int J Mol Sci
Date: Apr. 07, 2021
PubMed ID: 33917059
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