クローディン2

クローディン2（英: claudin-2）は、約23 kDa（キロダルトン）の膜タンパク質である。細胞膜を4回貫通しており、N末端とC末端は細胞質にある。C末端のチロシン-バリンを含む保存されたPDZ結合モチーフを介してタイトジャンクション裏打ちタンパク質のZO-1と結合する^[5]。

CLDN2

PDBに登録されている構造

PDB

オルソログ検索: RCSB PDBe PDBj

PDBのIDコード一覧
4YYX

識別子

記号

CLDN2, claudin 2, OAZON

外部ID

OMIM: 300520 MGI: 1276110 HomoloGene: 9621 GeneCards: CLDN2

遺伝子の位置 (ヒト)

染色体	X染色体^[1]

バンド	データ無し	開始点	106,900,164 bp^[1]
バンド	データ無し	終点	106,930,861 bp^[1]

遺伝子の位置 (マウス)

染色体	X染色体 (マウス)^[2]

バンド	データ無し	開始点	138,701,577 bp^[2]
バンド	データ無し	終点	138,712,135 bp^[2]

遺伝子オントロジー
分子機能	• 血漿タンパク結合 • identical protein binding • 構造分子活性
細胞の構成要素	• 細胞結合 • integral component of membrane • bicellular tight junction • 細胞膜 • 膜
生物学的プロセス	• calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules
出典:Amigo / QuickGO

オルソログ

種

ヒト

マウス

Entrez


9075


12738

Ensembl


ENSG00000165376


ENSMUSG00000047230

UniProt


P57739


O88552

RefSeq
(mRNA)


NM_020384 NM_001171092 NM_001171095


NM_016675

RefSeq
(タンパク質)


NP_001164563 NP_001164566 NP_065117


NP_057884

場所
(UCSC)

Chr X: 106.9 – 106.93 Mb

Chr X: 138.7 – 138.71 Mb

PubMed検索

^[3]

^[4]

ウィキデータ

閲覧/編集ヒト

閲覧/編集マウス

機能と疾患

クローディン2は、クローディンファミリーの一つでタイトジャンクションの主要構成成分である。特に、肝臓や腎臓に発現が多い^[6]^[7]。leakyタイプのクローディンに分類され、カチオンをよく通す^[8]^[9]。

クローディン2のノックアウトマウスは一見正常だが、腎臓の近位尿細管のタイトジャンクションにおける水と塩化ナトリウムの再吸収が低下しているため、塩負荷時の飲水量が上昇する^[10]。

発見の経緯

クローディン2は1998年に京都大学の月田承一郎らのグループによって報告された^[6]。

脚注

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000165376 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000047230 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
^ Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol, 147(6): 1351-63, 1999. (PMID 10601346)
^ ^a ^b Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita Sh. Claudin-1 and-2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol, 141(7): 1539-50, 1998. (PMID 9647647)
^ Morita K, Sasaki H, Fujimoto K, Furuse M, Tsukita Sh. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA, 96(2): 511-6, 1999. (PMID 9892664)
^ Furuse M, Furuse K, Sasaki H, Tsukita Sh. Conversion of zolulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol, 153(2): 263-72, 2001. (PMID 11309408)
^ Amasheh S, Meiri N, Gitter AH, Schöneberg T, Mankertz J, Schulzke JD, Fromm M. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J Cell Sci, 115(Pt 24): 4969-76, 2002. (PMID 12432083)
^ Muto S, Hata M, Taniguchi J, Tsuruoka S, Moriwaki K, Saitou M, Furuse K, Sasaki H, Fujimura A, Imai M, Kusano E, Tsukita Sh, Furuse M. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc Natl Acad Sci USA, 107(7): 8011-6, 2010. (PMID 20385797)

参考文献

“Tight junctions of the blood-brain barrier”. Cell. Mol. Neurobiol. 20 (1): 57–76. (2000). doi:10.1023/A:1006995910836. PMID (10690502).
“The roles of claudin superfamily proteins in paracellular transport”. Traffic 2 (2): 93–8. (2001). doi:10.1034/j.1600-0854.2001.020203.x. PMID (11247307).
“Multifunctional strands in tight junctions”. Nat. Rev. Mol. Cell Biol. 2 (4): 285–93. (2001). doi:10.1038/35067088. PMID (11283726).
“Claudin-based barrier in simple and stratified cellular sheets”. Curr. Opin. Cell Biol. 14 (5): 531–6. (2002). doi:10.1016/S0955-0674(02)00362-9. PMID (12231346).
“Tight junction proteins”. Prog. Biophys. Mol. Biol. 81 (1): 1–44. (2003). doi:10.1016/S0079-6107(02)00037-8. PMID (12475568).
“Role of claudins in tumorigenesis”. Adv. Drug Deliv. Rev. 57 (6): 919–28. (2005). doi:10.1016/j.addr.2005.01.006. PMID (15820559).
“HIV tat and neurotoxicity”. Microbes Infect. 8 (5): 1347–57. (2006). doi:10.1016/j.micinf.2005.11.014. PMID (16697675).
“Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus”. PLOS Pathog. 3 (8): e108. (2007). doi:10.1371/journal.ppat.0030108. PMC 1959368. PMID (17784784).
“Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin”. J. Cell Biol. 141 (7): 1539–50. (1998). doi:10.1083/jcb.141.7.1539. PMC 2132999. PMID (9647647).
“SEMP1, a senescence-associated cDNA isolated from human mammary epithelial cells, is a member of an epithelial membrane protein superfamily”. Gene 226 (2): 285–95. (1999). doi:10.1016/S0378-1119(98)00553-8. PMID (9931503).
“Manner of interaction of heterogeneous claudin species within and between tight junction strands”. J. Cell Biol. 147 (4): 891–903. (1999). doi:10.1083/jcb.147.4.891. PMC 2156154. PMID (10562289).
“Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins”. J. Cell Biol. 147 (6): 1351–63. (1999). doi:10.1083/jcb.147.6.1351. PMC 2168087. PMID (10601346).
“Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer”. Hum. Genet. 107 (3): 249–56. (2000). doi:10.1007/s004390000375. PMID (11071387).
“Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases”. J. Biol. Chem. 276 (30): 28204–11. (2001). doi:10.1074/jbc.M103083200. PMID (11382769).
“Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule”. J. Biol. Chem. 277 (1): 455–61. (2002). doi:10.1074/jbc.M109005200. PMID (11689568).
“A systems proteomics view of the endogenous human claudin protein family”. J Proteome Res 15 (2): 339–359. (2015). doi:10.1021/acs.jproteome.5b00769. PMC 4777318. PMID (26680015).

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000165376 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000047230 - Ensembl, May 2017

[3] Human PubMed Reference:

[4] Mouse PubMed Reference:

[5] Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol, 147(6): 1351-63, 1999. (PMID 10601346)

[furuse-6] Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita Sh. Claudin-1 and-2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol, 141(7): 1539-50, 1998. (PMID 9647647)

[7] Morita K, Sasaki H, Fujimoto K, Furuse M, Tsukita Sh. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA, 96(2): 511-6, 1999. (PMID 9892664)

[8] Furuse M, Furuse K, Sasaki H, Tsukita Sh. Conversion of zolulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol, 153(2): 263-72, 2001. (PMID 11309408)

[9] Amasheh S, Meiri N, Gitter AH, Schöneberg T, Mankertz J, Schulzke JD, Fromm M. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J Cell Sci, 115(Pt 24): 4969-76, 2002. (PMID 12432083)

[10] Muto S, Hata M, Taniguchi J, Tsuruoka S, Moriwaki K, Saitou M, Furuse K, Sasaki H, Fujimura A, Imai M, Kusano E, Tsukita Sh, Furuse M. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc Natl Acad Sci USA, 107(7): 8011-6, 2010. (PMID 20385797)

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