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Structure and function of the PLAA/Ufd3-p97/Cdc48 complex.

Liyan Qiu¹, Natasha Pashkova, John R Walker

¹Structural Genomics Consortium, Department of Physiology, University of Toronto, Toronto, Ontario M5G 1L7,Canada.

The Journal of Biological Chemistry

|November 6, 2009

Summary

This summary is machine-generated.

Phospholipase A2-activating protein (PLAA) interacts with p97 ATPase to regulate ubiquitin levels. The crystal structure reveals a conserved binding site crucial for some, but not all, PLAA functions in the ubiquitin system.

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Area of Science:

Cellular Biology
Biochemistry
Structural Biology

Background:

PLAA is involved in ubiquitin system processes, including maintaining ubiquitin levels.
The mechanism of PLAA's role in ubiquitin homeostasis is not fully understood.
PLAA's C-terminal PUL domain interacts with the AAA ATPase p97.

Purpose of the Study:

To elucidate the structural basis of the p97-PLAA interaction.
To understand the functional significance of this interaction in the ubiquitin system.

Main Methods:

High-resolution crystal structure determination of the p97-PLAA complex.
Analysis of conserved residues and binding interfaces.
Functional characterization of yeast Doa1 mutants disrupting the interaction.

Main Results:

The crystal structure reveals the PUL domain of PLAA forms an Armadillo-containing domain with a conserved, positively charged ridge.
This ridge binds the C-terminus of p97, specifically burying p97-Tyr(805).
Yeast mutants disrupting this interaction show partially reduced ubiquitin levels and some altered growth phenotypes.

Conclusions:

The p97-PLAA interaction is structurally defined and functionally important for a subset of PLAA-dependent processes.
This structural insight provides a framework for understanding PLAA's role in the ubiquitin system.
The interaction is critical for maintaining optimal ubiquitin levels and cellular growth in specific contexts.