BIOMAT Database Logo BIOMAT Database Logo

Identification of P2X2/P2X4/P2X6 heterotrimeric receptors using atomic force microscopy (AFM) imaging. 2014

Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, United Kingdom; Department of Physiology, School of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.

Seven P2X purinergic receptor subunits have been identified: P2X1-P2X7. The overlapping expression of P2X2, P2X4 and P2X6 subunits has been shown in different cell types, and functional analysis of P2X receptors in Leydig cells suggests that the three subunits might interact. Here, His6-tagged P2X2, HA-tagged P2X4 and FLAG-tagged P2X6 subunits were co-expressed in tsA 201 cells. After sequential co-immunoprecipitation using anti-HA and anti-FLAG beads, all three subunits were present, demonstrating their interaction. Atomic force microscopy (AFM) imaging revealed receptors that were specifically decorated by both an anti-His6 antibody and an anti-HA Fab fragment, indicating the presence of a P2X2/4/6 heterotrimer. To our knowledge, this is the first report of a P2X receptor containing three different subunits.

UI MeSH Term Description Entries
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D055503 Protein Multimerization The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS. Protein Dimerization,Protein Heteromultimerizaton,Protein Multimer Assembly,Protein Trimerization,Assembly, Protein Multimer,Dimerization, Protein,Heteromultimerizaton, Protein,Heteromultimerizatons, Protein,Multimer Assembly, Protein,Multimerization, Protein,Trimerization, Protein
D057809 HEK293 Cells A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5. 293T Cells,HEK 293 Cell Line,HEK 293 Cells,Human Embryonic Kidney Cell Line 293,Human Kidney Cell Line 293,293 Cell, HEK,293 Cells, HEK,293T Cell,Cell, 293T,Cell, HEK 293,Cell, HEK293,Cells, 293T,Cells, HEK 293,Cells, HEK293,HEK 293 Cell,HEK293 Cell
D058469 Receptors, Purinergic P2X A subclass of purinergic P2 receptors that signal by means of a ligand-gated ion channel. They are comprised of three P2X subunits which can be identical (homotrimeric form) or dissimilar (heterotrimeric form). P2X Purinoceptor,P2X Purinoceptors,P2X Receptors, Purinergic,Purinergic P2X Receptors,Purinoceptor, P2X,Purinoceptors, P2X
D058476 Receptors, Purinergic P2X2 A purinergic P2X neurotransmitter receptor involved in sensory signaling of TASTE PERCEPTION, chemoreception, visceral distension and NEUROPATHIC PAIN. The receptor comprises three P2X2 subunits. The P2X2 subunits also have been found associated with P2X3 RECEPTOR subunits in a heterotrimeric receptor variant. P2X2 Purinoceptor,P2X2 Purinoceptors,P2X2 Receptor,Purinergic Receptor P2X, Ligand-Gated Ion Channel, 2,P2X2 Receptors, Purinergic,Purinergic P2X2 Receptors,Purinoceptor, P2X2,Purinoceptors, P2X2,Receptor, P2X2
D058848 Receptors, Purinergic P2X4 A widely distributed purinergic P2X receptor subtype that plays a role in pain sensation. P2X4 receptors found on MICROGLIA cells may also play a role in the mediation of allodynia-related NEUROPATHIC PAIN. P2X4 Purinoceptor,P2X4 Receptor,Purinergic Receptor P2X, Ligand-Gated Ion Channel, 4,P2X4 Receptors, Purinergic,Purinergic P2X4 Receptors,Purinoceptor, P2X4,Receptor, P2X4
D018048 Receptors, Purinergic P2 A class of cell surface receptors for PURINES that prefer ATP or ADP over ADENOSINE. P2 purinergic receptors are widespread in the periphery and in the central and peripheral nervous system. ADP Receptors,ATP Receptors,P2 Purinoceptors,Purinergic P2 Receptors,Receptors, ADP,Receptors, ATP,ADP Receptor,ATP Receptor,P2 Purinoceptor,Receptor, Purinergic P2,P2 Receptor, Purinergic,P2 Receptors, Purinergic,Purinergic P2 Receptor,Purinoceptor, P2,Purinoceptors, P2,Receptor, ADP,Receptor, ATP
D018625 Microscopy, Atomic Force A type of scanning probe microscopy in which a probe systematically rides across the surface of a sample being scanned in a raster pattern. The vertical position is recorded as a spring attached to the probe rises and falls in response to peaks and valleys on the surface. These deflections produce a topographic map of the sample. Atomic Force Microscopy,Force Microscopy,Scanning Force Microscopy,Atomic Force Microscopies,Force Microscopies,Force Microscopies, Scanning,Force Microscopy, Scanning,Microscopies, Atomic Force,Microscopies, Force,Microscopies, Scanning Force,Microscopy, Force,Microscopy, Scanning Force,Scanning Force Microscopies

Related Publications

Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize.
March 2005, The Journal of biological chemistry,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Imaging collagen II using atomic force microscopy (AFM).
October 2010, Cold Spring Harbor protocols,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Imaging fibroblast cells using atomic force microscopy (AFM).
October 2010, Cold Spring Harbor protocols,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Imaging articular cartilage tissue using atomic force microscopy (AFM).
October 2010, Cold Spring Harbor protocols,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Atomic force microscopy (AFM).
February 2008, Current protocols in microbiology,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Quantification of bacterial adhesion forces using atomic force microscopy (AFM).
March 2000, Journal of microbiological methods,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Force and Compliance Measurements on Living Cells Using Atomic Force Microscopy (AFM).
January 2004, Biological procedures online,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Imaging cellulose using atomic force microscopy.
January 2012, Methods in molecular biology (Clifton, N.J.),
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
Ultrastructural pathology of varicocele spermatozoa by using atomic force microscopy (AFM).
January 2001, Archives of andrology,
Ligia S Antonio, and Andrew P Stewart, and Wamberto A Varanda, and J Michael Edwardson
[Application of atomic force microscopy (AFM) in ophthalmology].
January 2012, Klinika oczna,
Copied contents to your clipboard!