CNIH3 Membrane Protein Introduction

Introduction of CNIH3

Protein cornichon homolog 3 (CNIH-3), also known as cornichon family AMPA receptor auxiliary protein 3, is an AMPA receptor (AMPAR) binding proteins that promote receptor trafficking and markedly slow AMPAR deactivation in heterologous cells. The related pathways of CNIH-3 include metabolism of proteins and transport to the golgi and subsequent modification. Gene Ontology annotations associated with this gene include channel regulator activity. An important paralog of this gene is CNIH2.

Basic Information of CNIH3
Protein Name	Protein cornichon homolog 3
Gene Name	CNIH3
Aliases	CNIH-3, Cornichon family AMPA receptor auxiliary protein 3
Organism	Homo sapiens (Human)
UniProt ID	Q8TBE1
Transmembrane Times	3
Length (aa)	160
Sequence	MAFTFAAFCYMLSLVLCAALIFFAIWHIIAFDELRTDFKSPIDQCNPVHARERLRNIERICFLLRKLVLPEYSIHSLFCIMFLCAQEWLTLGLNVPLLFYHFWRYFHCPADSSELAYDPPVVMNADTLSYCQKEAWCKLAFYLLSFFYYLYCMIYTLVSS

Function of CNIH3 Membrane Protein

CNIH3 is involved in diseases such as schizophrenia. Protein cornichon homolog 3 regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). CNIH3 promotes their targeting to cell membrane and synapses and regulates their gating properties by modulating their activation, deactivation, and desensitization rates.

Fig.1 Protein network of human CNIH3.

Application of CNIH3 Membrane Protein in Literature

Nelson E.C., et al. Evidence of CNIH3 involvement in opioid dependence. Mol Psychiatry. 2016, 21(5): 608-14. PubMed ID: 26239289

The article reveals that CNIH3 is involved in the opioid dependence. These findings complement previous studies involving the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid glutamate system.
Shanks N.F., et al. Molecular dissection of the interaction between the AMPA receptor and cornichon homolog-3. J Neurosci. 2014, 34(36): 12104-20. PubMed ID: 25186755

Authors in this group identified a mutant CNIH-3 which preserves AMPAR binding ability but attenuates the activity of gating regulation.
Brown P.M., et al. Stargazin, and cornichon-3 relieve polyamine block of AMPA receptors by enhancing blocker permeation. J Gen Physiol. 2018, 150(1): 67-82. PubMed ID: 29222130

The article indicates that γ2 and CNIH-3 relieve channel block by facilitating the blocker's exit rates from the open channel.
Hawken N.M., et al. Engineering defined membrane-embedded elements of AMPA receptor induces opposing gating modulation by cornichon 3 and stargazin. J Physiol. 2017, 595(20): 6517-6539. PubMed ID: 28815591

This article focuses on the role of AMPA-type ionotropic glutamate receptors in the excitatory synaptic transmission. It shows that the membrane-embedded elements of AMPA receptor induce opposing gating regulation by cornichon 3 and stargazin.
Herring B.E., et al. Cornichon proteins determine the subunit composition of synaptic AMPA receptors. Neuron. 2013, 77(6): 1083-96. PubMed ID: 23522044

This article reports that Cornichon-3 protein may play a role in the determination of the subunit composition of synaptic AMPA receptors.

CNIH3 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-CNIH3 antibody development services.

As a leading service provider, Creative Biolabs is proud to present our professional service in membrane protein preparation and help you with the research of membrane proteins. Please do not hesitate to inquire us for more details.

Reference

Utsunomiya YT, et al. (2013). Detecting loci under recent positive selection in dairy and beef cattle by combining different genome-wide scan methods. PLoS One. 8(5): e64280.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

	USA: Europe: Germany:
	Call us at: USA: UK: Germany:
	Fax:
	Email: