TRPM6 Membrane Protein Introduction

Introduction of TRPM6

Transient receptor potential cation channel subfamily M member 6 (TRPM6), encoded by the gene TRPM6, is a member of TRP family of cation channels. TRPM6 is an Mg²⁺ -permeable channel, mainly expressed in the apical membrane of distal convoluted tubule and brush-border membrane of absorptive cells in the duodenum. TRPM6 is an extraordinary protein comprising two distinct functional moieties: an ion channel segment and an α-type serine/threonine kinase domain. Generally, TRPM6 cannot efficiently form functional channels by itself and needs to assemble with TRPM7. There are seven variants produced by alternative splicing of TRPM6 gene.

Basic Information of TRPM6
Protein Name	Transient receptor potential cation channel subfamily M member 6
Gene Name	TRPM6
Aliases	HSH, HMGX, HOMG, CHAK2, HOMG1
Organism	Homo sapiens (Human)
UniProt ID	Q9BX84
Transmembrane Times	6
Length (aa)	2022
Sequence	MKEQPVLERLQSQKSWIKGVFDKRECSTIIPSSKNPHRCTPVCQVCQNLIRCYCGRLIGDHAGIDYSWTISAAKGKESEQWSVEKHTTKSPTDTFGTINFQDGEHTHHAKYIRTSYDTKLDHLLHLMLKEWKMELPKLVISVHGGIQNFTMPSKFKEIFSQGLVKAAETTGAWIITEGINTGVSKHVGDALKSHSSHSLRKIWTVGIPPWGVIENQRDLIGKDVVCLYQTLDNPLSKLTTLNSMHSHFILSDDGTVGKYGNEMKLRRNLEKYLSLQKIHCRSRQGVPVVGLVVEGGPNVILSVWETVKDKDPVVVCEGTGRAADLLAFTHKHLADEGMLRPQVKEEIICMIQNTFNFSLKQSKHLFQILMECMVHRDCITIFDADSEEQQDLDLAILTALLKGTNLSASEQLNLAMAWDRVDIAKKHILIYEQHWKPDALEQAMSDALVMDRVDFVKLLIEYGVNLHRFLTIPRLEELYNTKQGPTNTLLHHLVQDVKQHTLLSGYRITLIDIGLVVEYLIGRAYRSNYTRKHFRALYNNLYRKYKHQRHSSGNRNESAESTLHSQFIRTAQPYKFKEKSIVLHKSRKKSKEQNVSDDPESTGFLYPYNDLLVWAVLMKRQKMAMFFWQHGEEATVKAVIACILYRAMAHEAKESHMVDDASEELKNYSKQFGQLALDLLEKAFKQNERMAMTLLTYELRNWSNSTCLKLAVSGGLRPFVSHTCTQMLLTDMWMGRLKMRKNSWLKIIISIILPPTILTLEFKSKAEMSHVPQSQDFQFMWYYSDQNASSSKESASVKEYDLERGHDEKLDENQHFGLESGHQHLPWTRKVYEFYSAPIVKFWFYTMAYLAFLMLFTYTVLVEMQPQPSVQEWLVSIYIFTNAIEVVREICISEPGKFTQKVKVWISEYWNLTETVAIGLFSAGFVLRWGDPPFHTAGRLIYCIDIIFWFSRLLDFFAVNQHAGPYVTMIAKMTANMFYIVIIMAIVLLSFGVARKAILSPKEPPSWSLARDIVFEPYWMIYGEVYAGEIDVCSSQPSCPPGSFLTPFLQAVYLFVQYIIMVNLLIAFFNNVYLDMESISNNLWKYNRYRYIMTYHEKPWLPPPLILLSHVGLLLRRLCCHRAPHDQEEGDVGLKLYLSKEDLKKLHDFEEQCVEKYFHEKMEDVNCSCEERIRVTSERVTEMYFQLKEMNEKVSFIKDSLLSLDSQVGHLQDLSALTVDTLKVLSAVDTLQEDEALLAKRKHSTCKKLPHSWSNVICAEVLGSMEIAGEKKYQYYSMPSSLLRSLAGGRHPPRVQRGALLEITNSKREATNVRNDQERQETQSSIVVSGVSPNRQAHSKYGQFLLVPSNLKRVPFSAETVLPLSRPSVPDVLATEQDIQTEVLVHLTGQTPVVSDWASVDEPKEKHEPIAHLLDGQDKAEQVLPTLSCTPEPMTMSSPLSQAKIMQTGGGYVNWAFSEGDETGVFSIKKKWQTCLPSTCDSDSSRSEQHQKQAQDSSLSDNSTRSAQSSECSEVGPWLQPNTSFWINPLRRYRPFARSHSFRFHKEEKLMKICKIKNLSGSSEIGQGAWVKAKMLTKDRRLSKKKKNTQGLQVPIITVNACSQSDQLNPEPGENSISEEEYSKNWFTVSKFSHTGVEPYIHQKMKTKEIGQCAIQISDYLKQSQEDLSKNSLWNSRSTNLNRNSLLKSSIGVDKISASLKSPQEPHHHYSAIERNNLMRLSQTIPFTPVQLFAGEEITVYRLEESSPLNLDKSMSSWSQRGRAAMIQVLSREEMDGGLRKAMRVVSTWSEDDILKPGQVFIVKSFLPEVVRTWHKIFQESTVLHLCLREIQQQRAAQKLIYTFNQVKPQTIPYTPRFLEVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEITPTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRKLKLPDLKRNDYSPERINSTFGLEIKIESAEEPPARETGRNSPEDDMQL

Function of TRPM6 Membrane Protein

As a transient receptor potential ion channel, TRPM6 plays a crucial role in magnesium homeostasis and is essential for magnesium transport in epithelial cells. In addition, it is required for active magnesium absorption in the kidney and gut. Heterologously expressed TRPM6 can form an Mg²⁺- and Ca²⁺-permeable channel, which is regulated by Mg²⁺ and blocked by ruthenium red. TRPM6 mutations cause hypomagnesemia with secondary hypocalcemia (HSH), an autosomal recessive disorder due to a dysfunction of intestinal magnesium absorption and consequent magnesium deficiency. It has been documented that missense mutations in TRPC6 are responsible for a form of familial focal segmental glomerulosclerosis (FSGS) with several typical manifestation, including proteinuria, hypertension, renal insufficiency, and eventually kidney failure. Therefore, TRPC6 may represent a useful therapeutic target in treating chronic kidney disease.

Fig.1 Schematic representation of TRPM6 structure in the plasma membrane.

Application of TRPM6 Membrane Protein in Literature

Luongo F., et al. TRPM6 is Essential for Magnesium Uptake and Epithelial Cell Function in the Colon. Nutrients. 2018, 10(6). pii: E784. PubMed ID: 29912157

This article demonstrates that TRPM7 cannot replace TRPM6, and that both TRPM6/7 complexes and TRPM6/7-mediated Mg²⁺ absorption are essential for normal human epithelial colon cells.
Morgan C.P., et al. TRPV6, TRPM6 and TRPM7 Do Not Contribute to Hair-Cell Mechanotransduction. Front Cell Neurosci. 2018, 12:41. PubMed ID: 29515374

This article suggests that TRPM6, TRPV6, and TRPM7 are not possible to be the pore-forming subunit of the transduction channel in hair-cell.
Komiya Y., et al. A Nonredundant Role for the TRPM6 Channel in Neural Tube Closure. Sci Rep. 2017, 7(1):15623. PubMed ID: 29142255

This article demonstrates that both TRPM6 and TRPM7 channels function cooperatively but they show distinct roles during neural tube closure.
Chubanov V., et al. Epithelial magnesium transport by TRPM6 is essential for prenatal development and adult survival. Elife. 2016, 5. pii: e20914. PubMed ID: 27991852

This article suggests that TRPM6 is essential for the maintenance of organismal magnesium ion balance, as it is crucial for prenatal development and survival to adulthood.
Saraç M., et al. Magnesium-permeable TRPM6 polymorphisms in patients with meningomyelocele. Springerplus. 2016, 5(1):1703. PubMed ID: 27757375

This article reveals that genetic variations in the magnesium ion-permeable TRPM6 ion channel may be associated with etiopathogenesis of meningomyelocele during embryonic development.

TRPM6 Preparation Options

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