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Tubulin as a binding partner of the heag2 voltage-gated potassium channel.
- Source :
- Journal of Membrane Biology; Apr2008, Vol. 222 Issue 3, p115-125, 11p, 1 Black and White Photograph, 1 Diagram, 1 Chart, 6 Graphs
- Publication Year :
- 2008
-
Abstract
- The aim of this work was to investigate interactions of the human ether-a-go-go channel heag2 with human brain proteins. For this, we used heag2-GST fusion proteins in pull-down assays with brain proteins and mass spectrometry, as well as coimmunoprecipitation. We identified tubulin and heat shock 70 proteins as binding to intracellular C-terminal regions of the channel. To study functional effects, heag2 channels were expressed in Xenopus laevis oocytes for two-electrode voltage clamping. Coexpression of alpha-tubulin or the application of colchicine significantly prolonged channel activation times. Application at different times of colchicine gave similar results. The data suggest that colchicine application and tubulin expression do not affect heag2 trafficking and that tubulin may associate with the channel to cause functional effects. Coexpression of heat shock 70 proteins had no functional effect on the channel. The role of tubulin in the cell cytoskeleton suggests a link for the heag2 channel in tubulin-dependent physiological functions, such as cellular proliferation. [ABSTRACT FROM AUTHOR]
- Subjects :
- BRAIN
TUBULINS
POTASSIUM channels
PROTEINS
CELL proliferation
AMINO acids
ANIMAL experimentation
ANTINEOPLASTIC agents
BIOCHEMISTRY
BIOLOGICAL transport
CARRIER proteins
CELL lines
COLCHICINE
COMPARATIVE studies
CYTOLOGICAL techniques
DOCUMENTATION
MASS spectrometry
MOLECULAR probes
PHENOMENOLOGY
RESEARCH methodology
MEDICAL cooperation
NERVE tissue proteins
OVUM
RECOMBINANT proteins
RESEARCH
RESEARCH funding
TRANSFERASES
VERTEBRATES
EVALUATION research
PHARMACODYNAMICS
PHYSIOLOGY
Subjects
Details
- Language :
- English
- ISSN :
- 00222631
- Volume :
- 222
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- Journal of Membrane Biology
- Publication Type :
- Academic Journal
- Accession number :
- 32785831
- Full Text :
- https://doi.org/10.1007/s00232-008-9104-x