TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals

URN to cite this document:

urn:nbn:de:bvb:355-epub-360189 Copy

DOI to cite this document:

10.5283/epub.36018 Copy

Stöhr, H. ; Heisig, J. B. ; Benz, P. M. ; Schöberl, S. ; Milenkovic, V. M. ; Strauss, O. ; Aartsen, W. . ; Wijnholds, J. ; Weber, Bernhard H. F. ; Schulz, H. L.

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Date of publication of this fulltext: 04 Aug 2017 08:07

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Details

Item type:	Article
Journal or Publication Title:	The Journal of Neuroscience
Publisher:	Society for Neuroscience
Volume:	29
Number of Issue or Book Chapter:	21
Page Range:	pp. 6809-6818
Date:	2009
Institutions:	Medicine > Lehrstuhl für Humangenetik
Identification Number:	Value Type 10.1523/JNEUROSCI.5546-08.2009 DOI 19474308 PubMed ID
Dewey Decimal Classification:	600 Technology > 610 Medical sciences Medicine
Status:	Published
Refereed:	Yes, this version has been refereed
Created at the University of Regensburg:	Partially
Item ID:	36018

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Abstract

Photoreceptor ribbon synapses release glutamate in response to graded changes in membrane potential evoked by vast, logarithmically scalable light intensities. Neurotransmitter release is modulated by intracellular calcium levels. Large Ca2+-dependent chloride currents are important regulators of synaptic transmission from photoreceptors to second-order neurons; the molecular basis underlying ...

Abstract

Photoreceptor ribbon synapses release glutamate in response to graded changes in membrane potential evoked by vast, logarithmically scalable light intensities. Neurotransmitter release is modulated by intracellular calcium levels. Large Ca2+-dependent chloride currents are important regulators of synaptic transmission from photoreceptors to second-order neurons; the molecular basis underlying these currents is unclear. We cloned human and mouse TMEM16B, a member of the TMEM16 family of transmembrane proteins, and show that it is abundantly present in the photoreceptor synaptic terminals in mouse retina. TMEM16B colocalizes with adaptor proteins PSD95, VELI3, and MPP4 at the ribbon synapses and contains a consensus PDZ class I binding motif capable of interacting with PDZ domains of PSD95. Furthermore, TMEM16B is lost from photoreceptor membranes of MPP4-deficient mice. This suggests that TMEM16B is a novel component of a presynaptic protein complex recruited to specialized plasma membrane domains of photoreceptors. TMEM16B confers Ca2+-dependent chloride currents when overexpressed in mammalian cells as measured by halide sensitive fluorescent protein assays and whole-cell patch-clamp recordings. The compartmentalized localization and the electrophysiological properties suggest TMEM16B to be a strong candidate for the long sought-after Ca2+-dependent chloride channel in the photoreceptor synapse.

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Metadata last modified: 17 Dec 2020 11:10

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