PLEC Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 1MB8 , 2ODU , 2ODV , 3F7P , 3PDY , 3PE0 , 4GDO , 4Q58 , 4Q59 , 2N03 , 5J1H , 5J1G , 5J1I
Identifikatori Aliasi PLEC Vanjski ID-jevi OMIM : 601282 MGI : 1277961 HomoloGene : 384 GeneCards : PLEC Ortolozi Vrste Čovjek Miš Entrez Ensembl UniProt RefSeq (mRNK) RefSeq (bjelančevina) Lokacija (UCSC) Chr 8: 143.92 – 143.98 Mb Chr 15: 76.06 – 76.12 Mb PubMed pretraga[ 3] [ 4] Wikipodaci
Plektin je gigantski protein koji je kod ljudi kodiran genom PLC . U [[ćelija (biologija)|ćelijama gotovo svih sisara djeluje kao link između tri glavne komponente citoskeleta : aktinsih mikrofilamenata, mikrotubula i srednjih filamenata .[ 5] Osim toga, plektin povezuje citoskelet s spojevima nađenim u plazmamembrani koji strukturno povezuju različite ćelije. Držanjem ovih različitih mreža zajedno plektin igra važnu ulogu u održavanju mehaničkog integriteta i viskoelastičnih svojstava tkiva .[ 6]
Dužina polipeptidnog lanca je 4.684 aminokiseline , а molekulska težina 531.791 Da .[ 7]
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LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ
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QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR
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SIEEFRAKIE RARSDEGQLS PATRGAYRDC LGRLDLQYAK LLNSSKARLR
SLESLHSFVA AATKELMWLN EKEEEEVGFD WSDRNTNMTA KKESYSALMR
ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ WSWMLQLCCC
IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL
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EAQEAVTRLE AQHQALVTLW HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT
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EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK
EAQAVPATLP ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL
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KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP KVQSGSESVI
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EVELASRVKA EAEAAREKQR ALQALEELRL QAEEAERRLR QAEVERARQV
QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV AQLREEAERR
AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ
ELIRLRAETE QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE
MEVLLASKAR AEEESRSTSE KSKQRLEAEA GRFRELAEEA ARLRALAEEA
KRQRQLAEED AARQRAEAER VLAEKLAAIG EATRLKTEAE IALKEKEAEN
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RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK
EKMQAVQEAT RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG
FQRTLEAERQ RQLEMSAEAE RLKLRVAEMS RAQARAEEDA QRFRKQAEEI
GEKLHRTELA TQEKVTLVQT LEIQRQQSDH DAERLREAIA ELEREKEKLQ
QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL QRERFIEQEK
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EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE
EVTASQVAAT KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI
LSAEELQRLA QGHTTVDELA RREDVRHYLQ GRSSIAGLLL KATNEKLSVY
AALQRQLLSP GTALILLEAQ AASGFLLDPV RNRRLTVNEA VKEGVVGPEL
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DTVRRALRGA NVIAGVWLEE AGQKLSIYNA LKKDLLPSDM AVALLEAQAG
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RRAFEETQID IPGGGSHGGS TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV
TKERMIIIII EIIEKTEIIR QQGLASYDYV RRRLTAEDLF EARIISLETY
NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT LSIYQALKKG
LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR
LGFHLPLEVA YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR
CRRDDGTGQL LLPLSDARKL TFRGLRKQIT MEELVRSQVM DEATALQLRE
GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT KERLSVYQAM KKGIIRPGTA
FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK LLSAERAVTG
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IDRSALDQYR AGTLSITEFA DMLSGNAGGF RSRSSSVGSS SSYPISPAVS
RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV DNITGQRLLE
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TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ
RGTVDARTAQ KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL
LEAAAQSTKG YYSPYSVSGS GSTAGSRTGS RTGSRAGSRR GSFDATGSGF
SMTFSSSSYS SSGYGRRYAS GSSASLGGPE SAVA
Plektin može postojati u ćelijama kao nekoliko alternativno prerađenih izoformi , svih oko 500 kDa i > 4000 aminokiselina .[ 8] [ 9] Smatra se da je struktura plektina dimerna , koja se sastoji od središnje upredene zavojnice od alfa-heliksa koja povezuje dva velika globulasta domena (po jedan na svakom kraju). Ovi globulastii domeni odgovorni su za povezivanje plektina sa različitim citoskeletnim ciljevima.Karboksi-terminalni domen sastoji se od šest visoko homolognih ponavljajućih regija. Poznato je da se poddomen između regija pet i šest ovog domena povezuje s međufaznim vlaknima citokeratin i vimentin . Na suprotnom kraju proteina, u N-terminalnom domenu, regija je definirana kao odgovorna za vezivanje za aktin .[ 10] Tačna kristalna struktura ovog aktin -vezujućeg domena (ABD) utvrđena 2004., kod miševa i pokazano je da se sastoji od dva kalponin homologna (CH) domena.[ 11] Plektin se eksprimira u gotovo svim tkivima sisara. U srčanom i skeletnim mišićima , plektin je lokaliziran na specijalizirane entitete poznate kao Z-diskovi .[ 12] Plektin veže nekoliko proteina, uključujući vinkulin , DES ,[ 13] aktin [ 6] [ 14] fodrin,[ 6] [ 14] microtubule-associating proteins,[ 6] [ 14] jedarni laminin B,[ 6] [ 14] SPTAN1 ,[ 15] [ 16] vimentin [ 15] [ 16] [ 17] i ITGB4 .[ 6] [ 14]
Studije koje su koristile plektinske nokaut-miševe rasvijetlile su funkcije plektina. Mladi su uginuli 2-3 dana nakon rođenja, a ti miševi su pokazali izražene abnormalnosti na koži, uključujući degeneraciju keratinocita . Skeletna i srčanomišićna tkiva također su značajno pogođena. Srčani interkalarni diskovi su se razgradili i sarkomere nepravilno oblikovane, a primijećeno je i unutarćelijsko nakupljanje aberantno izoliranih komponenti snopova miofibrila i Z-diskova . Ekspresija vinkulina u mišićnim ćelijama bila je izrazito smanjena.[ 18]
Korištenjem zlatne imunoelektronske mikroskopije, imunoblotiranja i imunofluoscencije , eksperimentalno otkriveno je da se plektin povezuje sa sve tri glavne komponente citoskeleta . U mišićima , plektin se veže za periferiju Z-diskova,[ 13] i zajedno sa proteinom među vlaknima dezmina može formirati bočne veze među susjednim Z-diskovima . Čini se da ova interakcija između plektinskih i dezminskih intermedijarnih niti olakšava blisku vezu miofibrila i mitohondrija , kako na Z-diskovima, tako i duž ostatka sarkomera .[ 19] Plectin također funkcionira tako da povezuje citoskelet s međućelijskim vezama , kao što su dezmosomi i hemidezmosomi , koji povezuju mreže među vlaknastih ćelija između njih. Otkriveno je da se plektin lokalizira u desmosomima, a studije in vitro pokazale su da može stvoriti mostove između dezmosomskih proteina, dezmoplakina i međuprostornih niti.[ 20] U hemidezmosomima je pokazano da plektin stupa u interakciju s podjedinicama integrina β4 plaka hemidezmozoma i funkcionira na način stezanja kako bi povezao srednji filament citokeratin sa spojem.[ 21]
Mutacije u PLEC -u povezane su sa epidermiolisis bulbosa (buloznom epidermolizom) sa mišićnom distrofijom .[ 22] Nedavno je predložena misens varijanta PLEC-a, kao uzrok pretkomorske fibrilacije u nekim populacijama .[ 23] Zabilježeno je i izolirano nekompaktiranje lijeve komore koje prati epidermolisis bullosa simplex s mišićnom distrofijom.[ 24]
Plektin je predložrn da bude biomarker za rak gušterače .[ 25] [ 26] Kao normalni citoplazmatski protein, plektin se također eksprimira u ćelijskim membranama adenokarcinoma gušteračnog kanala (PDAC) i može upotrebiti kao cilj PDAC ćelija .[ 25]
^ a b c GRCh38: Ensembl release 89: ENSG00000178209 - Ensembl , maj 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022565 - Ensembl , maj 2017
^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ Svitkina TM, Verkhovsky AB, Borisy GG (Nov 1996). "Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton" . The Journal of Cell Biology . 135 (4): 991–1007. doi :10.1083/jcb.135.4.991 . PMC 2133373 . PMID 8922382 .
^ a b c d e f Wiche G (Sep 1998). "Role of plectin in cytoskeleton organization and dynamics" (abstract) . Journal of Cell Science . 111 (17): 2477–86. doi :10.1242/jcs.111.17.2477 . PMID 9701547 .
^ "UniProt, Q15149" (jezik: engleski). Pristupljeno 20. 9. 2021 .
^ "Archived copy" . Arhivirano s originala , 5. 3. 2016. Pristupljeno 13. 4. 2015 .CS1 održavanje: arhivirana kopija u naslovu (link )
^ Zong, N. C.; Li, H; Li, H; Lam, M. P.; Jimenez, R. C.; Kim, C. S.; Deng, N; Kim, A. K.; Choi, J. H.; Zelaya, I; Liem, D; Meyer, D; Odeberg, J; Fang, C; Lu, H. J.; Xu, T; Weiss, J; Duan, H; Uhlen, M; Yates Jr, 3rd; Apweiler, R; Ge, J; Hermjakob, H; Ping, P (2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase" . Circulation Research . 113 (9): 1043–53. doi :10.1161/CIRCRESAHA.113.301151 . PMC 4076475 . PMID 23965338 .
^ Winter L, Wiche G (Jan 2013). "The many faces of plectin and plectinopathies: pathology and mechanisms". Acta Neuropathologica . 125 (1): 77–93. doi :10.1007/s00401-012-1026-0 . PMID 22864774 . S2CID 12429741 .
^ Sevcík J, Urbániková L, Kost'an J, Janda L, Wiche G (maj 2004). "Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin" . European Journal of Biochemistry / FEBS . 271 (10): 1873–84. doi :10.1111/j.1432-1033.2004.04095.x . PMID 15128297 .
^ Zernig G, Wiche G (Jul 1985). "Morphological integrity of single adult cardiac myocytes isolated by collagenase treatment: immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin". European Journal of Cell Biology . 38 (1): 113–22. PMID 2992982 .
^ a b Hijikata T, Murakami T, Imamura M, Fujimaki N, Ishikawa H (Mar 1999). "Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers". Journal of Cell Science . 112 (6): 867–76. doi :10.1242/jcs.112.6.867 . PMID 10036236 .
^ a b c d e Steinböck FA, Wiche G (Feb 1999). "Plectin: a cytolinker by design" . Biological Chemistry . 380 (2): 151–8. doi :10.1515/BC.1999.023 . PMID 10195422 . S2CID 46726381 .
^ a b Herrmann H, Wiche G (Jan 1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin" . The Journal of Biological Chemistry . 262 (3): 1320–5. doi :10.1016/S0021-9258(19)75789-5 . PMID 3027087 .
^ a b Brown MJ, Hallam JA, Liu Y, Yamada KM, Shaw S (Jul 2001). "Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin" . Journal of Immunology . 167 (2): 641–5. doi :10.4049/jimmunol.167.2.641 . PMID 11441066 .
^ Favre B, Schneider Y, Lingasamy P, Bouameur JE, Begré N, Gontier Y, Steiner-Champliaud MF, Frias MA, Borradori L, Fontao L (maj 2011). "Plectin interacts with the rod domain of type III intermediate filament proteins desmin and vimentin". European Journal of Cell Biology . 90 (5): 390–400. doi :10.1016/j.ejcb.2010.11.013 . PMID 21296452 .
^ Andrä K, Lassmann H, Bittner R, Shorny S, Fässler R, Propst F, Wiche G (Dec 1997). "Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture" . Genes & Development . 11 (23): 3143–56. doi :10.1101/gad.11.23.3143 . PMC 316746 . PMID 9389647 .
^ Reipert S, Steinböck F, Fischer I, Bittner RE, Zeöld A, Wiche G (Nov 1999). "Association of mitochondria with plectin and desmin intermediate filaments in striated muscle". Experimental Cell Research . 252 (2): 479–91. doi :10.1006/excr.1999.4626 . PMID 10527638 .
^ Huber O (Sep 2003). "Structure and function of desmosomal proteins and their role in development and disease" . Cellular and Molecular Life Sciences . 60 (9): 1872–90. doi :10.1007/s00018-003-3050-7 . PMID 14523549 . S2CID 11557417 .
^ Sonnenberg A, Liem RK (Jun 2007). "Plakins in development and disease". Experimental Cell Research . 313 (10): 2189–203. doi :10.1016/j.yexcr.2007.03.039 . PMID 17499243 .
^ Bardhan, Ajoy; Bruckner-Tuderman, Leena; Chapple, Iain L. C.; Fine, Jo-David; Harper, Natasha; Has, Cristina; Magin, Thomas M.; Marinkovich, M. Peter; Marshall, John F.; McGrath, John A.; Mellerio, Jemima E. (24. 9. 2020). "Epidermolysis bullosa" . Nature Reviews Disease Primers (jezik: engleski). 6 (1): 78. doi :10.1038/s41572-020-0210-0 . ISSN 2056-676X . PMID 32973163 . S2CID 221861310 .
^ Thorolfsdottir, Rosa B.; Sveinbjornsson, Gardar; Sulem, Patrick; Helgadottir, Anna; Gretarsdottir, Solveig; Benonisdottir, Stefania; Magnusdottir, Audur; Davidsson, Olafur B.; Rajamani, Sridharan; Roden, Dan M.; Darbar, Dawood; Pedersen, Terje R.; Sabatine, Marc S.; Jonsdottir, Ingileif; Arnar, David O.; Thorsteinsdottir, Unnur; Gudbjartsson, Daniel F.; Holm, Hilma; Stefansson, Kari (2017). "A Missense Variant in PLEC Increases Risk of Atrial Fibrillation" . Journal of the American College of Cardiology . 70 (17): 2157–2168. doi :10.1016/j.jacc.2017.09.005 . PMC 5704994 . PMID 29050564 .
^ Villa CR, Ryan TD, Collins JJ, Taylor MD, Lucky AW, Jefferies JL (Feb 2015). "Left ventricular non-compaction cardiomyopathy associated with epidermolysis bullosa simplex with muscular dystrophy and PLEC1 mutation". Neuromuscular Disorders . 25 (2): 165–8. doi :10.1016/j.nmd.2014.09.011 . PMID 25454730 . S2CID 25193440 .
^ a b Kelly KA, Bardeesy N, Anbazhagan R, Gurumurthy S, Berger J, Alencar H, Depinho RA, Mahmood U, Weissleder R (Apr 2008). "Targeted nanoparticles for imaging incipient pancreatic ductal adenocarcinoma" . PLOS Medicine . 5 (4): e85. doi :10.1371/journal.pmed.0050085 . PMC 2292750 . PMID 18416599 .
^ Bausch D, Thomas S, Mino-Kenudson M, Fernández-del CC, Bauer TW, Williams M, Warshaw AL, Thayer SP, Kelly KA (Jan 2011). "Plectin-1 as a novel biomarker for pancreatic cancer" . Clinical Cancer Research . 17 (2): 302–9. doi :10.1158/1078-0432.CCR-10-0999 . PMC 3044444 . PMID 21098698 .
Pfendner E, Rouan F, Uitto J (Apr 2005). "Progress in epidermolysis bullosa: the phenotypic spectrum of plectin mutations" . Experimental Dermatology . 14 (4): 241–9. doi :10.1111/j.0906-6705.2005.00324.x . PMID 15810881 . S2CID 27756698 .
Foisner R, Traub P, Wiche G (maj 1991). "Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin" . Proceedings of the National Academy of Sciences of the United States of America . 88 (9): 3812–6. Bibcode :1991PNAS...88.3812F . doi :10.1073/pnas.88.9.3812 . PMC 51543 . PMID 2023931 .
Herrmann H, Wiche G (Jan 1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin" . The Journal of Biological Chemistry . 262 (3): 1320–5. doi :10.1016/S0021-9258(19)75789-5 . PMID 3027087 .
Malecz N, Foisner R, Stadler C, Wiche G (Apr 1996). "Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site" . The Journal of Biological Chemistry . 271 (14): 8203–8. doi :10.1074/jbc.271.14.8203 . PMID 8626512 .
Liu CG, Maercker C, Castañon MJ, Hauptmann R, Wiche G (Apr 1996). "Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)" . Proceedings of the National Academy of Sciences of the United States of America . 93 (9): 4278–83. Bibcode :1996PNAS...93.4278L . doi :10.1073/pnas.93.9.4278 . PMC 39526 . PMID 8633055 .
Gache Y, Chavanas S, Lacour JP, Wiche G, Owaribe K, Meneguzzi G, Ortonne JP (maj 1996). "Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy" . The Journal of Clinical Investigation . 97 (10): 2289–98. doi :10.1172/JCI118671 . PMC 507309 . PMID 8636409 .
Smith FJ, Eady RA, Leigh IM, McMillan JR, Rugg EL, Kelsell DP, Bryant SP, Spurr NK, Geddes JF, Kirtschig G, Milana G, de Bono AG, Owaribe K, Wiche G, Pulkkinen L, Uitto J, McLean WH, Lane EB (Aug 1996). "Plectin deficiency results in muscular dystrophy with epidermolysis bullosa". Nature Genetics . 13 (4): 450–7. doi :10.1038/ng0896-450 . PMID 8696340 . S2CID 3096988 .
McLean WH, Pulkkinen L, Smith FJ, Rugg EL, Lane EB, Bullrich F, Burgeson RE, Amano S, Hudson DL, Owaribe K, McGrath JA, McMillan JR, Eady RA, Leigh IM, Christiano AM, Uitto J (Jul 1996). "Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization" . Genes & Development . 10 (14): 1724–35. doi :10.1101/gad.10.14.1724 . PMID 8698233 .
Nikolic B, Mac Nulty E, Mir B, Wiche G (Sep 1996). "Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions" . The Journal of Cell Biology . 134 (6): 1455–67. doi :10.1083/jcb.134.6.1455 . PMC 2121005 . PMID 8830774 .
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PDB galerija
1mb8 : Crystal Structure of the actin binding domain of plectin
1sh5 : Crystal structure of actin-binding domain of mouse plectin
1sh6 : Crystal structure of actin-binding domain of mouse plectin
2odu : Crystal structure of a fragment of the plakin domain of plectin
2odv : Crystal structure of a fragment of the plakin domain of plectin, Cys to Ala mutant.
^ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase" . Circulation Research . 113 (9): 1043–1053. doi :10.1161/CIRCRESAHA.113.301151 . PMC 4076475 . PMID 23965338 .