Merritt Maduke

Title
Assistant Professor

Department
Molecular and Cellular Physiology

Research Interests
Molecular mechanisms of chloride channels studied by integration of structural and electrophysiological methods.

Email
maduke@stanford.edu

Phone
(650)723-9075

Fax
(650)725-8021

Address
Beckman B155
Mail Code: 5345

Faculty Research Description
Our laboratory is taking a multidisciplinary approach to study the molecular mechanisms by which chloride-selective ion channels function. These remarkable membrane proteins are crucial to a wide variety of physiologic and pathophysiologic processes, including neuronal signaling, hippocampal development, skeletal muscle repolarization, endosomal and epithelial ion transport, and the bone remodeling process affected in osteoporosis. The major molecular family of chloride channels is known as the “CLC" family, and its members exhibit pore-properties and gating (opening/closing) mechanisms unprecedented in any other ion channel. Our starting point for understanding these functions at the molecular level is the recently solved crystal structure of a bacterial CLC homologue. We will integrate electrophysiological recording techniques (both macroscopic and single-channel) and molecular biology with direct biochemical and structural avenues of attack in order to decipher how these proteins work.

Mindell, J.A., Maduke, M., Miller, C., and Grigorieff, N. (2001). Projection structure of a ClC-type Cl- channel at 6.5 Å resolution. Nature 409, 219-223.

Mindell, J.A., Maduke, M. (2001). ClC chloride channels. Genome Biology 2(2):REVIEWS3003.

Maduke, M., Miller, C., and Mindell, J.A. (2000). A decade of ClC chloride channels: structure, mechanism, and many unsettled questions. Ann. Rev. Biophys. Biomol. Struct. 29, 411-438.

Maduke, M., Pheasant, D. J., and Miller, C. (1999). High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel. J. Gen. Physiol. 114, 713-722.

Maduke, M., Williams, C., and Miller, C. (1998). Formation of CLC-0 chloride channels from separated transmembrane and cytoplasmic domains. Biochemistry 37, 1315-1321.

Areas of Study
Membrane excitability
Molecular Neurobiology
SBRC
Ph.D.