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Related Experiment Video

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Dissection of Drosophila Ovaries

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Published on: October 19, 2006

Pendrin function and regulation in Xenopus oocytes.

Fabian R Reimold¹, John F Heneghan, Andrew K Stewart

¹Renal Division and Molecular and Vascular Medicine Unit, Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.

Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology

|November 26, 2011

Summary

This summary is machine-generated.

Pendrin (SLC26A4) mutations cause Pendred Syndrome and deafness. This study clarifies pendrin

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Xenopus Oocytes: Optimized Methods for Microinjection, Removal of Follicular Cell Layers, and Fast Solution Changes in Electrophysiological Experiments

Xenopus Oocytes: Optimized Methods for Microinjection, Removal of Follicular Cell Layers, and Fast Solution Changes in Electrophysiological Experiments

Published on: December 31, 2016

Area of Science:

Molecular biology
Genetics
Physiology

Background:

Mutations in SLC26A4 cause Pendred Syndrome and non-syndromic deafness.
The function and regulation of pendrin (SLC26A4 gene product) are not fully understood.

Purpose of the Study:

To extend the functional analysis of wildtype and mutant pendrin.
To investigate the regulation of pendrin and related SLC26 transporters.

Main Methods:

Functional analysis in Xenopus oocytes.
Isotopic flux assays.
Electrophysiology.
Protein localization studies.
Site-directed mutagenesis.

Main Results:

Pendrin mediates electroneutral anion exchange, insensitive to pH and DIDS.
Pendred Syndrome mutation E303Q causes loss-of-function with normal surface expression.
Mutagenesis at position 303 revealed E303K as a loss-of-function mutant.
Other SLC26 transporters (SLC26A2, SLC26A3, SLC26A6) are strongly inhibited by phorbol ester, unlike pendrin.
Phorbol ester inhibition of other SLC26 transporters is PKCδ-dependent, but not for pendrin.

Conclusions:

Pendrin exhibits unique transport properties and regulation compared to related SLC26 transporters.
Specific mutations in pendrin can lead to loss-of-function phenotypes relevant to Pendred Syndrome.
Pendrin's regulation by PKCδ differs significantly from other SLC26 family members.