NDLI: Roles of surface residues of intracellular domains of heag potassium channels

Content Provider	Springer Nature Link
Author	Stevens, Louisa Ju, Min Wray, Dennis
Copyright Year	2009
Abstract	Ether-a-go-go potassium channels have large intracellular regions containing ‘Per-Ant-Sim’ (PAS) and cyclic nucleotide binding (cNBD) domains at the N- and C-termini, respectively. In heag1 and heag2 channels, recent studies have suggested that the N- and C-terminal domains interact, and affect activation properties. Here, we have studied the effect of mutations of residues on the surfaces of PAS and cNBD domains. For this, we introduced alanine and lysine mutations in heag1 channels, and recorded currents by two-electrode voltage clamp. In both the PAS domain and the cNBD domain, contiguous areas of conserved residues on the surfaces of these domains were found which affected the activation kinetics of the channel. Next, we investigated possible effects of mutations on domain interactions of PAS and cNBD proteins in heag2 by co-expressing these domain proteins followed by analysis with native gels and western blotting. We found oligomeric association between these domains. Mutations F30A and A609K (on the surfaces of the PAS and cNBD domains, respectively) affected oligomeric compositions of these domains when proteins for PAS and cNBD domains were expressed together. Taken together, the data suggest that the PAS and cNBD domains form interacting oligomers that have roles in channel function.
Starting Page	523
Ending Page	532
Page Count	10
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	38
Issue Number	4
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-01-27
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Ion channels Potassium channels Electrophysiology Alanine scanning Ether-a-go-go channels Nanotechnology Neurobiology Membrane Biology Cell Biology Biophysics/Biomedical Physics Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Intracellular regions of potassium channels: Kv2.1 and heag

Role of intracellular domains in the function of the herg potassium channel

The voltage dependence of hEag currents is not determined solely by membrane-spanning domains

Crystal structure of the PAS domain of the hEAG potassium channel.

Structure and function of ion channels

The mechano-gated K2P channel TREK-1

Structure of the pore-helix of the hERG K+ channel

Brownian dynamics study of flux ratios in sodium channels

Impact of intracellular ion channels on cancer development and progression

Roles of surface residues of intracellular domains of heag potassium channels

Similar Documents

Intracellular regions of potassium channels: Kv2.1 and heag

Role of intracellular domains in the function of the herg potassium channel

The voltage dependence of hEag currents is not determined solely by membrane-spanning domains

Crystal structure of the PAS domain of the hEAG potassium channel.

Structure and function of ion channels

The mechano-gated K2P channel TREK-1

Structure of the pore-helix of the hERG K+ channel

Brownian dynamics study of flux ratios in sodium channels

Impact of intracellular ion channels on cancer development and progression

Roles of surface residues of intracellular domains of heag potassium channels