Dynamic regulation of the INAD signaling scaffold becomes crystal clear

Craig Montell

doi:10.1016/j.cell.2007.09.022

Dynamic regulation of the INAD signaling scaffold becomes crystal clear

Cell. 2007 Oct 5;131(1):19-21. doi: 10.1016/j.cell.2007.09.022.

Author

Craig Montell¹

Affiliation

¹ Departments of Biological Chemistry and Neuroscience, Center for Sensory Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. cmontell@jhmi.edu

PMID: 17923082
DOI: 10.1016/j.cell.2007.09.022

Abstract

PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in signal transduction cascades. Although PDZ modules are often viewed as passive participants, Mishra et al. (2007) now show that a PDZ domain in INAD, a scaffold protein in photoreceptor cells of the fruit fly, undergoes a light-dependent conformational change, which has important consequences for signaling and animal behavior.

Publication types

Comment

MeSH terms

Animals
Drosophila / anatomy & histology
Drosophila / chemistry
Drosophila Proteins / chemistry*
Drosophila Proteins / metabolism*
Eye Proteins / chemistry*
Eye Proteins / metabolism*
Light
Oxidation-Reduction
PDZ Domains
Photoreceptor Cells, Invertebrate / chemistry
Protein Conformation*
Vision, Ocular*

Substances

Drosophila Proteins
Eye Proteins
inaD protein, Drosophila