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Analysis of conformational changes in WASP using a split YFP.

Rina Pei Zhi Lim¹, Ashish Misra, Zhihao Wu

¹School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Republic of Singapore.

Biochemical and Biophysical Research Communications

|September 11, 2007

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Wiskott-Aldrich syndrome protein (WASP) autoinhibition is relieved by Nck1 and Toca-1. These proteins alter WASP conformation, promoting its active state for cellular functions.

Area of Science:

Cell Biology
Molecular Biology
Protein Conformation Studies

Background:

Wiskott-Aldrich syndrome protein (WASP) is regulated by autoinhibition, adopting a closed conformation.
Proteins interacting with WASP are proposed to relieve this autoinhibition.
Understanding WASP conformation is crucial for cellular signaling pathways.

Purpose of the Study:

To investigate the conformational changes of WASP.
To determine the role of WASP-interacting proteins in regulating WASP conformation.
To analyze how Nck1 and Toca-1 affect WASP autoinhibition.

Main Methods:

Utilized split Yellow Fluorescent Protein (YFP) complementation assay in Saccharomyces cerevisiae.
Constructed YFP-fused WASP variants (YFP1-154-WASP-YFP155-238).

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Assessed YFP fluorescence changes upon co-expression with WASP-interacting proteins (WIP, Toca-1, Nck1).

Main Results:

Intramolecular YFP complementation confirmed WASP's closed conformation.
WASP-interacting protein (WIP) enhanced YFP fluorescence, indicating interaction but not altered stability.
Toca-1 and Nck1 significantly reduced YFP fluorescence, even with WIP, suggesting conformational changes.
Nck1 and Toca-1 binding alters WASP conformation, relieving autoinhibition.

Conclusions:

The split YFP system effectively monitors WASP conformation.
Nck1 and Toca-1 are identified as novel regulators that relieve WASP autoinhibition.
These findings provide insights into the molecular mechanisms controlling WASP activation.