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In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
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Clathrin Adaptor Complex-interacting Protein Irc6 Functions through the Conserved C-Terminal Domain
Huajun Zhou1, Giancarlo Costaguta2, Gregory S Payne3
1Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.
Scientific Reports
|March 16, 2019
Summary
The yeast protein Irc6, essential for vesicle transport, requires its C-terminal amino acids for binding to AP-1. Its N-terminal domain also plays a role in AP-1-mediated transport, suggesting diverse cellular functions.
Area of Science:
- Cell biology
- Molecular biology
- Membrane trafficking
Background:
- Clathrin coats mediate vesicle formation and transport.
- Clathrin adaptors orchestrate coat assembly.
- Yeast Irc6 is an orthologue of human p34, linked to punctate palmoplantar keratoderma.
Purpose of the Study:
- Investigate the functional domains of yeast Irc6.
- Determine the role of Irc6 in AP-1-dependent transport.
- Explore the cellular functions of Irc6.
Main Methods:
- Site-directed mutagenesis to alter Irc6 C-terminus.
- Overexpression of Irc6 domains.
- Analysis of AP-1 binding and transport function.
- Genetic interaction analysis.
Main Results:
- The C-terminal two amino acids of Irc6 are essential for AP-1 binding and transport.
- Overexpression of the N-terminal domain partially rescues AP-1-mediated transport.
- Negative genetic interactions of irc6∆ mutants implicate Irc6 in membrane traffic and nuclear processes.
Conclusions:
- Irc6's C-terminus is critical for AP-1 interaction and function.
- Both N- and C-terminal domains contribute to Irc6's role in AP-1-mediated transport.
- Irc6 has diverse cellular roles beyond vesicle transport, potentially involving nuclear processes.
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