4WJW

Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3

Replaces:  4U9T

Summary for 4WJW

• Entry DOI: 10.2210/pdb4wjw/pdb
• Related: 4GNS 4IN3 4Q66
• Descriptor: Chitin biosynthesis protein CHS5, Chitin biosynthesis protein CHS6, CHITIN SYNTHASE 3, ... (4 entities in total)
• Functional Keywords: adaptor protein, cargo binding, vesicular trafficking, chitin synthase, biosynthetic protein, transport protein-transferase complex, transport protein/transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein : Q12114 P40955
• Total number of polymer chains: 3
• Total formula weight: 98978.52

Authors

Weiskoff, A.M.,Fromme, J.C. (deposition date: 2014-10-01, release date: 2014-10-15, Last modification date: 2023-09-27)

Primary citation

Weiskoff, A.M.,Fromme, J.C.
Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary.
Front Cell Dev Biol, 2:47-47, 2014

PubMed Abstract: Cells transport integral membrane proteins between organelles by sorting them into vesicles. Cargo adaptors act to recognize sorting signals in transmembrane cargos and to interact with coat complexes that aid in vesicle biogenesis. No coat proteins have yet been identified that generate secretory vesicles from the trans-Golgi network (TGN) to the plasma membrane, but the exomer complex has been identified as a cargo adaptor complex that mediates transport of several proteins in this pathway. Chs3, the most well-studied exomer cargo, cycles between the TGN and the plasma membrane in synchrony with the cell cycle, providing an opportunity to study regulation of proteins that cycle in response to signaling. Here we show that different segments of the Chs3 N-terminus mediate distinct trafficking steps. Residues 10-27, known to mediate retention, also appear to play a role in internalization. Residues 28-52 are involved in transport to the plasma membrane and recycling out of endosomes to prevent degradation in the vacuole. We also present the crystal structure of residues 10-27 bound to the exomer complex, suggesting different cargo adaptors could compete for binding to this segment, providing a potential mechanism for regulation.

PubMed: 25364754
DOI: 10.3389/fcell.2014.00047

Experimental method

X-RAY DIFFRACTION (2.59 Å)