KCNMB1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Calcium-activated potassium channel subunit beta-1''' is a [[protein]] that in humans is encoded by the ''KCNMB1'' [[gene]].<ref name="pmid8799178">{{cite journal | vauthors = Tseng-Crank J, Godinot N, Johansen TE, Ahring PK, Strøbaek D, Mertz R, Foster CD, Olesen SP, Reinhart PH | title = Cloning, expression, and distribution of a Ca(2+)-activated K+ channel beta-subunit from human brain | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 17 | pages = 9200–5 | date = Aug 1996 | pmid = 8799178 | pmc = 38619 | doi = 10.1073/pnas.93.17.9200 }}</ref><ref name="pmid9888999">{{cite journal | vauthors = Jiang Z, Wallner M, Meera P, Toro L | title = Human and rodent MaxiK channel beta-subunit genes: cloning and characterization | journal = Genomics | volume = 55 | issue = 1 | pages = 57–67 | date = Jan 1999 | pmid = 9888999 | pmc = | doi = 10.1006/geno.1998.5627 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: KCNMB1 potassium large conductance calcium-activated channel, subfamily M, beta member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3779| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Potassium large conductance calcium-activated channel, subfamily M, beta member 1
| HGNCid = 6285
| Symbol = KCNMB1
| AltSymbols =; K(VCA)beta; SLO-BETA; hslo-beta
| OMIM = 603951
| ECnumber = 
| Homologene = 3054
| MGIid = 1334203
| GeneAtlas_image1 = PBB_GE_KCNMB1_209948_at_tn.png
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0015269 |text = calcium-activated potassium channel activity}} {{GNF_GO|id=GO:0015459 |text = potassium channel regulator activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0006939 |text = smooth muscle contraction}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3779
    | Hs_Ensembl = ENSG00000145936
    | Hs_RefseqProtein = NP_004128
    | Hs_RefseqmRNA = NM_004137
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 169737745
    | Hs_GenLoc_end = 169749216
    | Hs_Uniprot = Q16558
    | Mm_EntrezGene = 16533
    | Mm_Ensembl = ENSMUSG00000020155
    | Mm_RefseqmRNA = NM_031169
    | Mm_RefseqProtein = NP_112446
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 33863286
    | Mm_GenLoc_end = 33871275
    | Mm_Uniprot = Q5SQK1
  }}
}}
'''Potassium large conductance calcium-activated channel, subfamily M, beta member 1''', also known as '''KCNMB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNMB1 potassium large conductance calcium-activated channel, subfamily M, beta member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3779| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit and the product of this gene, the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits.<ref name="entrez" /> Beta subunits (beta 1-4) are highly tissue specific in their expression, with beta-1 being present predominantly on vascular smooth muscle. Endothelial cells are not known to express beta-1 subunits. Beta-1 is also known to be expressed in urinary bladder and in some regions of the brain. Association of the beta-1 subunit with the BK channel increases the apparent Ca<sup>2+</sup> sensitivity of the channel and decreases voltage dependence.<ref name="TanoGollasch2014">{{cite journal|last1=Tano|first1=J.-Y.|last2=Gollasch|first2=M.|title=Hypoxia and ischemia-reperfusion: a BiK contribution?|journal=AJP: Heart and Circulatory Physiology|volume=307|issue=6|year=2014|pages=H811–H817|issn=0363-6135|doi=10.1152/ajpheart.00319.2014}}</ref>
{{PBB_Summary
| section_title =
| summary_text = MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit and the product of this gene, the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits.<ref name="entrez">{{cite web | title = Entrez Gene: KCNMB1 potassium large conductance calcium-activated channel, subfamily M, beta member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3779| accessdate = }}</ref>
}}


==See also==
== See also ==
* [[BK channel]]
* [[BK channel]]
* [[Voltage-gated potassium channel]]
* [[Voltage-gated potassium channel]]


==References==
== References ==
{{reflist|2}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}  
{{PBB_Further_reading
* {{cite journal | vauthors = Orio P, Rojas P, Ferreira G, Latorre R | title = New disguises for an old channel: MaxiK channel beta-subunits | journal = News in Physiological Sciences | volume = 17 | issue =  | pages = 156–61 | date = Aug 2002 | pmid = 12136044 | doi =  10.1152/nips.01387.2002}}
| citations =
* {{cite journal | vauthors = Knaus HG, Folander K, Garcia-Calvo M, Garcia ML, Kaczorowski GJ, Smith M, Swanson R | title = Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle | journal = The Journal of Biological Chemistry | volume = 269 | issue = 25 | pages = 17274–8 | date = Jun 1994 | pmid = 8006036 | doi =  }}
*{{cite journal | author=Orio P, Rojas P, Ferreira G, Latorre R |title=New disguises for an old channel: MaxiK channel beta-subunits. |journal=News Physiol. Sci. |volume=17 |issue=  |pages= 156-61 |year= 2002 |pmid= 12136044 |doi=  }}
* {{cite journal | vauthors = Meera P, Wallner M, Jiang Z, Toro L | title = A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels | journal = FEBS Letters | volume = 382 | issue = 1–2 | pages = 84–8 | date = Mar 1996 | pmid = 8612769 | doi = 10.1016/0014-5793(96)00151-2 }}
*{{cite journal | author=Knaus HG, Folander K, Garcia-Calvo M, ''et al.'' |title=Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle. |journal=J. Biol. Chem. |volume=269 |issue= 25 |pages= 17274-8 |year= 1994 |pmid= 8006036 |doi=  }}
* {{cite journal | vauthors = Dworetzky SI, Boissard CG, Lum-Ragan JT, McKay MC, Post-Munson DJ, Trojnacki JT, Chang CP, Gribkoff VK | title = Phenotypic alteration of a human BK (hSlo) channel by hSlobeta subunit coexpression: changes in blocker sensitivity, activation/relaxation and inactivation kinetics, and protein kinase A modulation | journal = The Journal of Neuroscience | volume = 16 | issue = 15 | pages = 4543–50 | date = Aug 1996 | pmid = 8764643 | doi =  }}
*{{cite journal | author=Meera P, Wallner M, Jiang Z, Toro L |title=A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels. |journal=FEBS Lett. |volume=382 |issue= 1-2 |pages= 84-8 |year= 1996 |pmid= 8612769 |doi= }}
* {{cite journal | vauthors = Valverde MA, Rojas P, Amigo J, Cosmelli D, Orio P, Bahamonde MI, Mann GE, Vergara C, Latorre R | title = Acute activation of Maxi-K channels (hSlo) by estradiol binding to the beta subunit | journal = Science | volume = 285 | issue = 5435 | pages = 1929–31 | date = Sep 1999 | pmid = 10489376 | doi = 10.1126/science.285.5435.1929 }}
*{{cite journal | author=Dworetzky SI, Boissard CG, Lum-Ragan JT, ''et al.'' |title=Phenotypic alteration of a human BK (hSlo) channel by hSlobeta subunit coexpression: changes in blocker sensitivity, activation/relaxation and inactivation kinetics, and protein kinase A modulation. |journal=J. Neurosci. |volume=16 |issue= 15 |pages= 4543-50 |year= 1996 |pmid= 8764643 |doi=  }}
* {{cite journal | vauthors = Meera P, Wallner M, Toro L | title = A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 10 | pages = 5562–7 | date = May 2000 | pmid = 10792058 | pmc = 25868 | doi = 10.1073/pnas.100118597 }}
*{{cite journal | author=Tseng-Crank J, Godinot N, Johansen TE, ''et al.'' |title=Cloning, expression, and distribution of a Ca(2+)-activated K+ channel beta-subunit from human brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 17 |pages= 9200-5 |year= 1996 |pmid= 8799178 |doi= }}
* {{cite journal | vauthors = Jin P, Weiger TM, Wu Y, Levitan IB | title = Phosphorylation-dependent functional coupling of hSlo calcium-dependent potassium channel and its hbeta 4 subunit | journal = The Journal of Biological Chemistry | volume = 277 | issue = 12 | pages = 10014–20 | date = Mar 2002 | pmid = 11790768 | doi = 10.1074/jbc.M107682200 }}
*{{cite journal | author=Jiang Z, Wallner M, Meera P, Toro L |title=Human and rodent MaxiK channel beta-subunit genes: cloning and characterization. |journal=Genomics |volume=55 |issue= 1 |pages= 57-67 |year= 1999 |pmid= 9888999 |doi= 10.1006/geno.1998.5627 }}
* {{cite journal | vauthors = Greenwood IA, Miller LJ, Ohya S, Horowitz B | title = The large conductance potassium channel beta-subunit can interact with and modulate the functional properties of a calcium-activated chloride channel, CLCA1 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 25 | pages = 22119–22 | date = Jun 2002 | pmid = 11994272 | doi = 10.1074/jbc.C200215200 }}
*{{cite journal | author=Valverde MA, Rojas P, Amigo J, ''et al.'' |title=Acute activation of Maxi-K channels (hSlo) by estradiol binding to the beta subunit. |journal=Science |volume=285 |issue= 5435 |pages= 1929-31 |year= 1999 |pmid= 10489376 |doi= }}
* {{cite journal | vauthors = Gollasch M, Tank J, Luft FC, Jordan J, Maass P, Krasko C, Sharma AM, Busjahn A, Bähring S | title = The BK channel beta1 subunit gene is associated with human baroreflex and blood pressure regulation | journal = Journal of Hypertension | volume = 20 | issue = 5 | pages = 927–33 | date = May 2002 | pmid = 12011654 | doi = 10.1097/00004872-200205000-00028 }}
*{{cite journal | author=Meera P, Wallner M, Toro L |title=A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 10 |pages= 5562-7 |year= 2000 |pmid= 10792058 |doi= 10.1073/pnas.100118597 }}
* {{cite journal | vauthors = Jin P, Weiger TM, Levitan IB | title = Reciprocal modulation between the alpha and beta 4 subunits of hSlo calcium-dependent potassium channels | journal = The Journal of Biological Chemistry | volume = 277 | issue = 46 | pages = 43724–9 | date = Nov 2002 | pmid = 12223479 | doi = 10.1074/jbc.M205795200 }}
*{{cite journal | author=Jin P, Weiger TM, Wu Y, Levitan IB |title=Phosphorylation-dependent functional coupling of hSlo calcium-dependent potassium channel and its hbeta 4 subunit. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10014-20 |year= 2002 |pmid= 11790768 |doi= 10.1074/jbc.M107682200 }}
* {{cite journal | vauthors = Mazzone JN, Kaiser RA, Buxton IL | title = Calcium-activated potassium channel expression in human myometrium: effect of pregnancy | journal = Proceedings of the Western Pharmacology Society | volume = 45 | issue = | pages = 184–6 | year = 2003 | pmid = 12434576 | doi =  }}
*{{cite journal | author=Greenwood IA, Miller LJ, Ohya S, Horowitz B |title=The large conductance potassium channel beta-subunit can interact with and modulate the functional properties of a calcium-activated chloride channel, CLCA1. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22119-22 |year= 2002 |pmid= 11994272 |doi= 10.1074/jbc.C200215200 }}
* {{cite journal | vauthors = Kudlacek PE, Pluznick JL, Ma R, Padanilam B, Sansom SC | title = Role of hbeta1 in activation of human mesangial BK channels by cGMP kinase | journal = American Journal of Physiology. Renal Physiology | volume = 285 | issue = 2 | pages = F289-94 | date = Aug 2003 | pmid = 12670831 | doi = 10.1152/ajprenal.00046.2003 }}
*{{cite journal | author=Gollasch M, Tank J, Luft FC, ''et al.'' |title=The BK channel beta1 subunit gene is associated with human baroreflex and blood pressure regulation. |journal=J. Hypertens. |volume=20 |issue= 5 |pages= 927-33 |year= 2002 |pmid= 12011654 |doi=  }}
* {{cite journal | vauthors = Qian X, Magleby KL | title = Beta1 subunits facilitate gating of BK channels by acting through the Ca2+, but not the Mg2+, activating mechanisms | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 17 | pages = 10061–6 | date = Aug 2003 | pmid = 12893878 | pmc = 187764 | doi = 10.1073/pnas.1731650100 }}
*{{cite journal | author=Jin P, Weiger TM, Levitan IB |title=Reciprocal modulation between the alpha and beta 4 subunits of hSlo calcium-dependent potassium channels. |journal=J. Biol. Chem. |volume=277 |issue= 46 |pages= 43724-9 |year= 2003 |pmid= 12223479 |doi= 10.1074/jbc.M205795200 }}
* {{cite journal | vauthors = Ransom CB, Liu X, Sontheimer H | title = Current transients associated with BK channels in human glioma cells | journal = The Journal of Membrane Biology | volume = 193 | issue = 3 | pages = 201–13 | date = Jun 2003 | pmid = 12962281 | doi = 10.1007/s00232-003-2019-7 }}
*{{cite journal | author=Mazzone JN, Kaiser RA, Buxton IL |title=Calcium-activated potassium channel expression in human myometrium: effect of pregnancy. |journal=Proc. West. Pharmacol. Soc. |volume=45 |issue= |pages= 184-6 |year= 2003 |pmid= 12434576 |doi= }}
* {{cite journal | vauthors = Hartness ME, Brazier SP, Peers C, Bateson AN, Ashford ML, Kemp PJ | title = Post-transcriptional control of human maxiK potassium channel activity and acute oxygen sensitivity by chronic hypoxia | journal = The Journal of Biological Chemistry | volume = 278 | issue = 51 | pages = 51422–32 | date = Dec 2003 | pmid = 14522958 | doi = 10.1074/jbc.M309463200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Fernández-Fernández JM, Tomás M, Vázquez E, Orio P, Latorre R, Sentí M, Marrugat J, Valverde MA | title = Gain-of-function mutation in the KCNMB1 potassium channel subunit is associated with low prevalence of diastolic hypertension | journal = The Journal of Clinical Investigation | volume = 113 | issue = 7 | pages = 1032–9 | date = Apr 2004 | pmid = 15057310 | pmc = 379324 | doi = 10.1172/JCI20347 }}
*{{cite journal | author=Kudlacek PE, Pluznick JL, Ma R, ''et al.'' |title=Role of hbeta1 in activation of human mesangial BK channels by cGMP kinase. |journal=Am. J. Physiol. Renal Physiol. |volume=285 |issue= 2 |pages= F289-94 |year= 2003 |pmid= 12670831 |doi= 10.1152/ajprenal.00046.2003 }}
* {{cite journal | vauthors = Leo MD, Bannister JP, Narayanan D, Nair A, Grubbs JE, Gabrick KS, Boop FA, Jaggar JH | title = Dynamic regulation of β1 subunit trafficking controls vascular contractility | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 111 | issue = 6 | pages = 2361–6 | date = Feb 2014 | pmid = 24464482 | doi = 10.1073/pnas.1317527111 | pmc=3926029}}
*{{cite journal | author=Qian X, Magleby KL |title=Beta1 subunits facilitate gating of BK channels by acting through the Ca2+, but not the Mg2+, activating mechanisms. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 17 |pages= 10061-6 |year= 2003 |pmid= 12893878 |doi= 10.1073/pnas.1731650100 }}
* {{cite journal | vauthors = Kuntamallappanavar G, Toro L, Dopico AM | title = Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels | journal = PLoS One | volume = 9 | issue = 10 | pages = e109306 | year = 2014 | pmid = 25275635 | doi = 10.1371/journal.pone.0109306 | pmc=4183656}}
*{{cite journal | author=Ransom CB, Liu X, Sontheimer H |title=Current transients associated with BK channels in human glioma cells. |journal=J. Membr. Biol. |volume=193 |issue= 3 |pages= 201-13 |year= 2004 |pmid= 12962281 |doi= 10.1007/s00232-003-2019-7 }}
*{{cite journal | author=Hartness ME, Brazier SP, Peers C, ''et al.'' |title=Post-transcriptional control of human maxiK potassium channel activity and acute oxygen sensitivity by chronic hypoxia. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51422-32 |year= 2004 |pmid= 14522958 |doi= 10.1074/jbc.M309463200 }}
*{{cite journal  | author=Fernández-Fernández JM, Tomás M, Vázquez E, ''et al.'' |title=Gain-of-function mutation in the KCNMB1 potassium channel subunit is associated with low prevalence of diastolic hypertension. |journal=J. Clin. Invest. |volume=113 |issue= 7 |pages= 1032-9 |year= 2004 |pmid= 15057310 |doi= 10.1172/JCI200420347 }}
}}
{{refend}}
{{refend}}


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{{Ion channels}}
{{Ion channels|g3}}
 
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{{membrane-protein-stub}}

Revision as of 02:00, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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Calcium-activated potassium channel subunit beta-1 is a protein that in humans is encoded by the KCNMB1 gene.[1][2][3]

Function

MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit and the product of this gene, the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits.[3] Beta subunits (beta 1-4) are highly tissue specific in their expression, with beta-1 being present predominantly on vascular smooth muscle. Endothelial cells are not known to express beta-1 subunits. Beta-1 is also known to be expressed in urinary bladder and in some regions of the brain. Association of the beta-1 subunit with the BK channel increases the apparent Ca2+ sensitivity of the channel and decreases voltage dependence.[4]

See also

References

  1. Tseng-Crank J, Godinot N, Johansen TE, Ahring PK, Strøbaek D, Mertz R, Foster CD, Olesen SP, Reinhart PH (Aug 1996). "Cloning, expression, and distribution of a Ca(2+)-activated K+ channel beta-subunit from human brain". Proceedings of the National Academy of Sciences of the United States of America. 93 (17): 9200–5. doi:10.1073/pnas.93.17.9200. PMC 38619. PMID 8799178.
  2. Jiang Z, Wallner M, Meera P, Toro L (Jan 1999). "Human and rodent MaxiK channel beta-subunit genes: cloning and characterization". Genomics. 55 (1): 57–67. doi:10.1006/geno.1998.5627. PMID 9888999.
  3. 3.0 3.1 "Entrez Gene: KCNMB1 potassium large conductance calcium-activated channel, subfamily M, beta member 1".
  4. Tano, J.-Y.; Gollasch, M. (2014). "Hypoxia and ischemia-reperfusion: a BiK contribution?". AJP: Heart and Circulatory Physiology. 307 (6): H811–H817. doi:10.1152/ajpheart.00319.2014. ISSN 0363-6135.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.