NDLI: The importance of serine 161 in the sodium channel β3 subunit for modulation of NaV1.2 gating

Content Provider	Springer Nature Link
Author	Merrick, Ellen C. Kalmar, Christopher L. Snyder, Sandy L. Cusdin, Fiona S. Yu, Ester J. Sando, Julianne J. Isakson, Brant E. Jackson, Antony P. Patel, Maj K.
Copyright Year	2009
Abstract	Voltage-gated sodium (Na) channels contribute to the regulation of cellular excitability due to their role in the generation and propagation of action potentials. They are composed of a pore-forming α subunit and are modulated by at least two of four distinct β subunits (β1–4). Recent studies have implicated a role for the intracellular domain of β subunits in modulating Na channel gating and trafficking. In β3, the intracellular domain contains a serine residue at position 161 that is replaced by an alanine in β1. In this study, we have probed the functional importance of β3S161 for modulating Na channel gating. Wild-type β3 and point mutations β3S161A or β3S161E were individually co-expressed in HEK 293 cells stably expressing human Nav1.2. WTβ3 expression increased Na current density, shifted steady-state inactivation in a depolarized direction, and accelerated the kinetics of recovery from inactivation of the Na current. Analogous effects were observed with β3S161E co-expression. In contrast, β3S161A abolished the shifts in steady-state inactivation and recovery from inactivation of the Na current, but did increase Na current density. Immunocytochemistry and Western blot experiments demonstrate membrane expression of WTβ3, β3S161E, and β3S161A, suggesting that the differences in Na channel gating were not due to disruptions in β subunit trafficking. These studies suggest that modification of β3S161 may be important in modulating Na-channel gating.
Starting Page	743
Ending Page	753
Page Count	11
File Format	PDF
ISSN	00316768
Journal	Pflügers Archiv
Volume Number	460
Issue Number	4
e-ISSN	14322013
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-10-06
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Sodium channels Electrophysiology Auxiliary β subunits Site directed mutagenesis Immunohistochemistry Human Physiology
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Clinical Biochemistry

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

The importance of serine 161 in the sodium channel β3 subunit for modulation of Nav1.2 gating

Modulation of Nav1.5 by β1- and β3-subunit co-expression in mammalian cells

The importance of serine 161 in the sodium channel beta3 subunit for modulation of Na(V)1.2 gating.

Determinants of the voltage dependence of G protein modulation within calcium channel β subunits

Kinetics and Gβγ modulation of Cav2.2 channels with different auxiliary β subunits

Cross-kingdom auxiliary subunit modulation of a voltage-gated sodium channel

The Sodium Channel β3-Subunit Induces Multiphasic Gating in NaV1.3 and Affects Fast Inactivation via Distinct Intracellular Regions

Regulation of wild-type and mutant KCNQ1/KCNE1 channels by tyrosine kinase

Cross-kingdom auxiliary subunit modulation of a voltage-gated sodium channel

The importance of serine 161 in the sodium channel β3 subunit for modulation of NaV1.2 gating

Similar Documents

The importance of serine 161 in the sodium channel β3 subunit for modulation of Nav1.2 gating

Modulation of Nav1.5 by β1- and β3-subunit co-expression in mammalian cells

The importance of serine 161 in the sodium channel beta3 subunit for modulation of Na(V)1.2 gating.

Determinants of the voltage dependence of G protein modulation within calcium channel β subunits

Kinetics and Gβγ modulation of Cav2.2 channels with different auxiliary β subunits

Cross-kingdom auxiliary subunit modulation of a voltage-gated sodium channel

The Sodium Channel β3-Subunit Induces Multiphasic Gating in NaV1.3 and Affects Fast Inactivation via Distinct Intracellular Regions

Regulation of wild-type and mutant KCNQ1/KCNE1 channels by tyrosine kinase

Cross-kingdom auxiliary subunit modulation of a voltage-gated sodium channel

The importance of serine 161 in the sodium channel β3 subunit for modulation of NaV1.2 gating