NDLI: Localization of the PIP2 Sensor of TRPV1 Ion Channels*

Content Provider	PubMed Central
Author	Ufret-vincenty, Carmen A. Klein, Rebecca M. Hua, Li Juan, Angueyra Gordon, Sharona E.
Abstract	Although a large number of ion channels are now believed to be regulated by phosphoinositides, particularly phosphoinositide 4,5-bisphosphate (PIP2), the mechanisms involved in phosphoinositide regulation are unclear. For the TRP superfamily of ion channels, the role and mechanism of PIP2 modulation has been especially difficult to resolve. Outstanding questions include: is PIP2 the endogenous regulatory lipid; does PIP2 potentiate all TRPs or are some TRPs inhibited by PIP2; where does PIP2 interact with TRP channels; and is the mechanism of modulation conserved among disparate subfamilies? We first addressed whether the PIP2 sensor resides within the primary sequence of the channel itself, or, as recently proposed, within an accessory integral membrane protein called Pirt. Here we show that Pirt does not alter the phosphoinositide sensitivity of TRPV1 in HEK-293 cells, that there is no FRET between TRPV1 and Pirt, and that dissociated dorsal root ganglion neurons from Pirt knock-out mice have an apparent affinity for PIP2 indistinguishable from that of their wild-type littermates. We followed by focusing on the role of the C terminus of TRPV1 in sensing PIP2. Here, we show that the distal C-terminal region is not required for PIP2 regulation, as PIP2 activation remains intact in channels in which the distal C-terminal has been truncated. Furthermore, we used a novel in vitro binding assay to demonstrate that the proximal C-terminal region of TRPV1 is sufficient for PIP2 binding. Together, our data suggest that the proximal C-terminal region of TRPV1 can interact directly with PIP2 and may play a key role in PIP2 regulation of the channel.
Related Links	http://dx.doi.org/10.1074/jbc.m110.192526
Ending Page	9698
Page Count	11
Starting Page	9688
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	11
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-03-18
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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

Localization of the PIP2 Sensor of TRPV1 Ion Channels

Lipid Agonism, The PIP2 Paradigm of Ligand-Gated Ion Channels

Dual effect of phosphatidylinositol (4,5)-bisphosphate PIP2 on Shaker K+ channels.

Dual Effect of Phosphatidyl (4,5)-Bisphosphate PIP2 on Shaker K+ Channels*

The Endoplasmic Reticulum of Dorsal Root Ganglion Neurons Contains Functional TRPV1 Channels*

Tunable Calcium Current through TRPV1 Receptor Channels* S⃞

Regulation of TRPV1 Ion Channel by Phosphoinositide (4,5)-Bisphosphate THE ROLE OF MEMBRANE ASYMMETRY

A Structural Determinant for the Control of PIP2 Sensitivity in G Protein-gated Inward Rectifier K+ Channels

Promiscuous Activation of Transient Receptor Potential Vanilloid 1 (TRPV1) Channels by Negatively Charged Intracellular Lipids THE KEY ROLE OF ENDOGENOUS PHOSPHOINOSITIDES IN MAINTAINING CHANNEL ACTIVITY

Localization of the PIP2 Sensor of TRPV1 Ion Channels*

Similar Documents

Localization of the PIP2 Sensor of TRPV1 Ion Channels

Lipid Agonism, The PIP2 Paradigm of Ligand-Gated Ion Channels

Dual effect of phosphatidylinositol (4,5)-bisphosphate PIP2 on Shaker K+ channels.

Dual Effect of Phosphatidyl (4,5)-Bisphosphate PIP2 on Shaker K+ Channels*

The Endoplasmic Reticulum of Dorsal Root Ganglion Neurons Contains Functional TRPV1 Channels*

Tunable Calcium Current through TRPV1 Receptor Channels* S⃞

Regulation of TRPV1 Ion Channel by Phosphoinositide (4,5)-Bisphosphate THE ROLE OF MEMBRANE ASYMMETRY

A Structural Determinant for the Control of PIP2 Sensitivity in G Protein-gated Inward Rectifier K+ Channels

Promiscuous Activation of Transient Receptor Potential Vanilloid 1 (TRPV1) Channels by Negatively Charged Intracellular Lipids THE KEY ROLE OF ENDOGENOUS PHOSPHOINOSITIDES IN MAINTAINING CHANNEL ACTIVITY

Localization of the PIP2 Sensor of TRPV1 Ion Channels*