KCNJ15: Difference between revisions

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{{Infobox_gene}}
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'''Potassium inwardly-rectifying channel, subfamily J, member 15''', also known as '''KCNJ15''' is a human [[gene]], which encodes the '''K<sub>ir</sub>4.2''' [[protein]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNJ15 potassium inwardly-rectifying channel, subfamily J, member 15| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3772| accessdate = }}</ref>
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== Function ==
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Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. '''K<sub>ir</sub>4.2''' is an integral membrane protein and inward-rectifier type potassium channel. '''K<sub>ir</sub>4.2''' has a greater tendency to allow potassium to flow into a cell rather than out of a cell. Three transcript variants encoding the same protein have been found for this gene.<ref name="entrez"/>
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Potassium inwardly-rectifying channel, subfamily J, member 15
| HGNCid = 6261
| Symbol = KCNJ15
| AltSymbols =; IRKK; KIR1.3; KIR4.2; MGC13584
| OMIM = 602106
| ECnumber = 
| Homologene = 1690
| MGIid = 1310000
| GeneAtlas_image1 = PBB_GE_KCNJ15_210119_at_tn.png
| GeneAtlas_image2 = PBB_GE_KCNJ15_211806_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005242 |text = inward rectifier potassium channel activity}} {{GNF_GO|id=GO:0005244 |text = voltage-gated ion channel activity}} {{GNF_GO|id=GO:0005267 |text = potassium channel activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}  
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3772
    | Hs_Ensembl = ENSG00000157551
    | Hs_RefseqProtein = NP_002234
    | Hs_RefseqmRNA = NM_002243
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 38550534
    | Hs_GenLoc_end = 38595618
    | Hs_Uniprot = Q99712
    | Mm_EntrezGene = 16516
    | Mm_Ensembl = ENSMUSG00000062609
    | Mm_RefseqmRNA = NM_001039056
    | Mm_RefseqProtein = NP_001034145
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 95366449
    | Mm_GenLoc_end = 95409058
    | Mm_Uniprot = Q3TNE6
  }}
}}
'''Potassium inwardly-rectifying channel, subfamily J, member 15''', also known as '''KCNJ15''' is a human [[gene]], which encodes the gene product '''Kir4.2'''.<ref name="entrez">{{cite web | title = Entrez Gene: KCNJ15 potassium inwardly-rectifying channel, subfamily J, member 15| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3772| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
The existing literature describing KCNJ15 and K<sub>ir</sub>4.2 is sparse. In spite of some initial channel nomenclature confusion, in which the gene was referred to as Kir1.3<ref name="Pearson et al. 1999">{{cite journal |vauthors=Pearson WL, Dourado M, Schreiber M, Salkoff L, Nichols CG |title=Expression of a functional Kir4 family inward rectifier K+ channel from a gene cloned from mouse liver |journal=J. Physiol. |volume=514 ( Pt 3) |issue= 3|pages=639–653 |year=1999 |pmid=9882736 |doi=10.1111/j.1469-7793.1999.639ad.x |pmc=2269105}}</ref> the channel was first cloned from human [[kidney]] by Shuck and coworkers in 1997.<ref name="Shuck et al. 1997">{{cite journal |vauthors=Shuck ME, Piser TM, Bock JH, Slightom JL, Lee KS, Bienkowski MJ |title=Cloning and characterization of two K+ inward rectifier (Kir) 1.1 potassium channel homologs from human kidney (Kir1.2 and Kir1.3) |journal=J. Biol. Chem. |volume=272 |issue=1 |pages=586–593 |year=1997 |pmid=8995301 |doi=10.1074/jbc.272.1.586}}</ref> Shortly thereafter it was shown that mutation of an extracellular [[lysine]] residue resulted in 6-fold increase in K<sup>+</sup> current.<ref name="Derst et al. 1998">{{cite journal |author=Derst C |title=A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary potassium) channels reveals a crucial residue for channel function in Kir1.3 channels |journal=J. Biol. Chem. |volume=273 |issue=37 |pages=23884–23891 |year=1998 |pmid=9727001 |doi=10.1074/jbc.273.37.23884 |name-list-format=vanc|author2=Wischmeyer E |author3=Preisig-Müller R |display-authors=3 |last4=Spauschus |first4=A |last5=Konrad |first5=M |last6=Hensen |first6=P |last7=Jeck |first7=N |last8=Seyberth |first8=HW |last9=Daut |first9=J}}</ref> Two years later, in 1999, voltage clamp measurements in [[xenopus]] [[oocytes]] found that intracellular acidification decreased the potassium current of K<sub>ir</sub>4.2. Also activation of protein kinase C decreased the current although in a non-reversible fashion. Furthermore, it was found that coexpression with related potassium channel [[KCNJ16|K<sub>ir</sub>5.1]], changed these results somewhat, which the authors concluded was likely to be a result of heterodimerization.<ref name="Pearson et al. 1999" /> Further voltage clamp investigations found the exact pH sensitivity (pK<sub>a</sub> = 7.1), open probability (high) and conductance of ~25 pS.<ref name="Pessia et al. 2001">{{cite journal |vauthors=Pessia M, Imbrici P, D'Adamo MC, Salvatore L, Tucker SJ |title=Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1 |journal=J. Physiol. |volume=532 |issue=Pt 2 |pages=359–367 |year=2001 |pmid=11306656 |doi=10.1111/j.1469-7793.2001.0359f.x |pmc=2278540}}</ref> In 2007 the channel was found to interact with the [[Calcium-sensing receptor]] in human kidney, using a yeast-two-hybrid system. This co-localization was verified at the protein level using both [[immunofluorescence]] techniques and [[immunoprecipitation|coimmunoprecipitation]] of K<sub>ir</sub>4.2 and the [[Calcium-sensing receptor]].<ref name="Huang et al. 2007">{{cite journal |author=Huang C |title=Interaction of the Ca2+-sensing receptor with the inwardly rectifying potassium channels Kir4.1 and Kir4.2 results in inhibition of channel function |journal=Am. J. Physiol. Renal Physiol. |volume=292 |issue=3 |pages=F1073–F1081 |year=2007 |pmid=17122384 |doi=10.1152/ajprenal.00269.2006 |name-list-format=vanc|author2=Sindic A |author3=Hill CE |display-authors=3 |last4=Hujer |first4=K. M. |last5=Chan |first5=K. W. |last6=Sassen |first6=M. |last7=Wu |first7=Z. |last8=Kurachi |first8=Y. |last9=Nielsen |first9=S.}}</ref> Also a mutational study of K<sub>ir</sub>4.2 has demonstrated that removal of a c-terminal [[tyrosine]] increased the K<sup>+</sup> current more than 10-fold.<ref name="Pearson et al. 2007">{{cite journal |vauthors=Pearson WL, Skatchkov SN, Eaton MJ, Nichols CG |title=C-terminal determinants of Kir4.2 channel expression |journal=J. Membr. Biol. |volume=213 |issue=3 |pages=187–193 |year=2006 |pmid=17468958 |doi=10.1007/s00232-006-0058-6}}</ref> Because the channel has a very high open probability, the authors of this last article conclude that this increase is mediated by increased trafficking of the protein to the membrane and not increased single-channel conductance. This same line of reasoning is applicable to the initial work of Derst and coworkers.<ref name="Derst et al. 1998" />
{{PBB_Summary
| section_title =  
| summary_text = Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein has a greater tendency to allow potassium to flow into a cell rather than out of a cell. Three transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: KCNJ15 potassium inwardly-rectifying channel, subfamily J, member 15| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3772| accessdate = }}</ref>
}}


The existing literature describing KCNJ15 and kir4.2 is sparse. In spite of some initial channel nomenclature confusion, in which the gene was refered to as kir1.3<ref name="Pearson et al. 1999">{{cite journal |author=Pearson WL, Dourado M, Schreiber M, Salkoff L, Nichols CG |title=Expression of a functional Kir4 family inward rectifier K+ channel from a gene cloned from mouse liver |journal=J. Physiol. (Lond.) |volume=514 ( Pt 3) |issue= |pages=639–53 |year=1999 |pmid=9882736}}</ref> the channel was first cloned from human [[kidney]] by Shuck and coworkers in 1997<ref name="Shuck et al. 1997">{{cite journal |author=Shuck ME, Piser TM, Bock JH, Slightom JL, Lee KS, Bienkowski MJ |title=Cloning and characterization of two K+ inward rectifier (Kir) 1.1 potassium channel homologs from human kidney (Kir1.2 and Kir1.3) |journal=J. Biol. Chem. |volume=272 |issue=1 |pages=586–93 |year=1997 |pmid=8995301}}</ref>. Shortly thereafter it was shown that mutation of an extracellular [[lysine]] residue resulted in 6-fold increase in K<sup>+</sup> current<ref name="Derst et al. 1998">{{cite journal |author=Derst C, Wischmeyer E, Preisig-Müller R, ''et al'' |title=A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary potassium) channels reveals a crucial residue for channel function in Kir1.3 channels |journal=J. Biol. Chem. |volume=273 |issue=37 |pages=23884–91 |year=1998 |pmid=9727001}}</ref>. Two years later, in 1999, voltage clamp measurements in [[xenopus]] [[oocytes]] found that intracellular acidification decreased the potassium current of Kir4.2. Also activation of protein kinase C decreased the current although in a non-reversible fashion. Furthermore it was found that coexpression with related potassium channel [[KCNJ16|kir5.1]], changed these results somewhat, which the authors concluded was likely to be a result of heterodimerization<ref name="Pearson et al. 1999" />. Further voltage clamp investigations found the exact pH sensitivity (pK<sub>a</sub> = 7.1), open probability (high) and conductance of ~25 pS<ref name="Pessia et al. 2001">{{cite journal |author=Pessia M, Imbrici P, D'Adamo MC, Salvatore L, Tucker SJ |title=Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1 |journal=J. Physiol. (Lond.) |volume=532 |issue=Pt 2 |pages=359–67 |year=2001 |pmid=11306656 |doi=}}</ref>. In 2007 the channel was found to interact with the [[Calcium-sensing receptor]] in human kidney, using a yeast-two-hybrid system. This co-localization was verified at the protein level using both [[immunofluorescence]] techniques and [[immunoprecipitation|coimmunoprecipitation]] of kir4.2 and the [[Calcium-sensing receptor]]<ref name="Huang et al. 2007">{{cite journal |author=Huang C, Sindic A, Hill CE, ''et al'' |title=Interaction of the Ca2+-sensing receptor with the inwardly rectifying potassium channels Kir4.1 and Kir4.2 results in inhibition of channel function |journal=Am. J. Physiol. Renal Physiol. |volume=292 |issue=3 |pages=F1073–81 |year=2007 |pmid=17122384 |doi=10.1152/ajprenal.00269.2006}}</ref>. Also a mutational study of kir4.2 has demonstrated that removal of a c-terminal [[tyrosine]] increased the K<sup>+</sup> current more than 10-fold<ref name="Pearson et al. 2007">{{cite journal |author=Pearson WL, Skatchkov SN, Eaton MJ, Nichols CG |title=C-terminal determinants of Kir4.2 channel expression |journal=J. Membr. Biol. |volume=213 |issue=3 |pages=187–93 |year=2006 |pmid=17468958 |doi=10.1007/s00232-006-0058-6}}</ref>. Because the channel has a very high open probability, the authors of this last article conclude that this increase is mediated by increased trafficking of the protein to the membrane and not increased single-channel conductance. This same line of reasoning is applicable to the initial work of Derst and coworkers<ref name="Derst et al. 1998" />.
==Interactions==
KCNJ15 has been shown to [[Protein-protein interaction|interact]] with [[Interleukin 16]].<ref name=pmid10479680>{{cite journal |last=Kurschner |first=C |authorlink= |last2=Yuzaki |first2=M |date=Sep 1999|title=Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein |journal=J. Neurosci. |volume=19 |issue=18 |pages=7770–80 | pmid = 10479680}}</ref>


==See also==
==See also==
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==References==
==References==
{{reflist|2}}
{{reflist}}


{{NLM content}}
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{{Membrane proteins}}
{{Ion channels|g3}}
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{{Ion channels}}
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Latest revision as of 02:18, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

n/a

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Potassium inwardly-rectifying channel, subfamily J, member 15, also known as KCNJ15 is a human gene, which encodes the Kir4.2 protein.[1]

Function

Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. Kir4.2 is an integral membrane protein and inward-rectifier type potassium channel. Kir4.2 has a greater tendency to allow potassium to flow into a cell rather than out of a cell. Three transcript variants encoding the same protein have been found for this gene.[1]

The existing literature describing KCNJ15 and Kir4.2 is sparse. In spite of some initial channel nomenclature confusion, in which the gene was referred to as Kir1.3[2] the channel was first cloned from human kidney by Shuck and coworkers in 1997.[3] Shortly thereafter it was shown that mutation of an extracellular lysine residue resulted in 6-fold increase in K+ current.[4] Two years later, in 1999, voltage clamp measurements in xenopus oocytes found that intracellular acidification decreased the potassium current of Kir4.2. Also activation of protein kinase C decreased the current although in a non-reversible fashion. Furthermore, it was found that coexpression with related potassium channel Kir5.1, changed these results somewhat, which the authors concluded was likely to be a result of heterodimerization.[2] Further voltage clamp investigations found the exact pH sensitivity (pKa = 7.1), open probability (high) and conductance of ~25 pS.[5] In 2007 the channel was found to interact with the Calcium-sensing receptor in human kidney, using a yeast-two-hybrid system. This co-localization was verified at the protein level using both immunofluorescence techniques and coimmunoprecipitation of Kir4.2 and the Calcium-sensing receptor.[6] Also a mutational study of Kir4.2 has demonstrated that removal of a c-terminal tyrosine increased the K+ current more than 10-fold.[7] Because the channel has a very high open probability, the authors of this last article conclude that this increase is mediated by increased trafficking of the protein to the membrane and not increased single-channel conductance. This same line of reasoning is applicable to the initial work of Derst and coworkers.[4]

Interactions

KCNJ15 has been shown to interact with Interleukin 16.[8]

See also

References

  1. ↑ 1.0 1.1 "Entrez Gene: KCNJ15 potassium inwardly-rectifying channel, subfamily J, member 15".
  2. ↑ 2.0 2.1 Pearson WL, Dourado M, Schreiber M, Salkoff L, Nichols CG (1999). "Expression of a functional Kir4 family inward rectifier K+ channel from a gene cloned from mouse liver". J. Physiol. 514 ( Pt 3) (3): 639–653. doi:10.1111/j.1469-7793.1999.639ad.x. PMC 2269105. PMID 9882736.
  3. ↑ Shuck ME, Piser TM, Bock JH, Slightom JL, Lee KS, Bienkowski MJ (1997). "Cloning and characterization of two K+ inward rectifier (Kir) 1.1 potassium channel homologs from human kidney (Kir1.2 and Kir1.3)". J. Biol. Chem. 272 (1): 586–593. doi:10.1074/jbc.272.1.586. PMID 8995301.
  4. ↑ 4.0 4.1 Derst C, Wischmeyer E, Preisig-Müller R, et al. (1998). "A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary potassium) channels reveals a crucial residue for channel function in Kir1.3 channels". J. Biol. Chem. 273 (37): 23884–23891. doi:10.1074/jbc.273.37.23884. PMID 9727001.
  5. ↑ Pessia M, Imbrici P, D'Adamo MC, Salvatore L, Tucker SJ (2001). "Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1". J. Physiol. 532 (Pt 2): 359–367. doi:10.1111/j.1469-7793.2001.0359f.x. PMC 2278540. PMID 11306656.
  6. ↑ Huang C, Sindic A, Hill CE, et al. (2007). "Interaction of the Ca2+-sensing receptor with the inwardly rectifying potassium channels Kir4.1 and Kir4.2 results in inhibition of channel function". Am. J. Physiol. Renal Physiol. 292 (3): F1073–F1081. doi:10.1152/ajprenal.00269.2006. PMID 17122384.
  7. ↑ Pearson WL, Skatchkov SN, Eaton MJ, Nichols CG (2006). "C-terminal determinants of Kir4.2 channel expression". J. Membr. Biol. 213 (3): 187–193. doi:10.1007/s00232-006-0058-6. PMID 17468958.
  8. ↑ Kurschner, C; Yuzaki, M (Sep 1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): 7770–80. PMID 10479680.

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

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