메뉴 건너뛰기




Volumn 4, Issue , 2014, Pages

Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric state

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; RNF213 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE;

EID: 84906766180     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep04442     Document Type: Article
Times cited : (89)

References (45)
  • 1
    • 0002725175 scopus 로고
    • Hypoplasia of the bilateral internal carotid arteries
    • Takeuchi, K. & Shimizu, K. Hypoplasia of the bilateral internal carotid arteries. Brain Nerve 9, 37-43 (1957).
    • (1957) Brain Nerve , vol.9 , pp. 37-43
    • Takeuchi, K.1    Shimizu, K.2
  • 2
    • 53449097960 scopus 로고    scopus 로고
    • Moyamoya disease: Current concepts and future perspectives
    • Kuroda, S. & Houkin, K. Moyamoya disease: current concepts and future perspectives. Lancet Neurol 7, 1056-1066, http://dx.doi.org/10.1016/S1474-4422(08)70240-0 (2008).
    • (2008) Lancet Neurol , vol.7 , pp. 1056-1066
    • Kuroda, S.1    Houkin, K.2
  • 3
    • 62749176396 scopus 로고    scopus 로고
    • Moyamoya disease and moyamoya syndrome
    • Scott, R. M. & Smith, E. R. Moyamoya disease and moyamoya syndrome. N. Engl. J. Med. 360, 1226-1237, http://dx.doi.org/10.1056/NEJMra0804622 (2009).
    • (2009) N. Engl. J. Med. , vol.360 , pp. 1226-1237
    • Scott, R.M.1    Smith, E.R.2
  • 4
    • 0014477593 scopus 로고
    • Cerebrovascular "moyamoya" disease. Disease showing abnormal net-like vessels in base of brain
    • Suzuki, J. & Takaku, A. Cerebrovascular "moyamoya" disease. Disease showing abnormal net-like vessels in base of brain. Arch. Neurol. 20, 288-299 (1969).
    • (1969) Arch. Neurol. , vol.20 , pp. 288-299
    • Suzuki, J.1    Takaku, A.2
  • 5
    • 0030715614 scopus 로고    scopus 로고
    • Guidelines for the diagnosis and treatment of spontaneous occlusion of the circle of Willis ('moyamoya' disease)
    • Research Committee on Spontaneous Occlusion of the Circle of Willis (Moyamoya Disease) of the Ministry of Health and Welfare, Japan
    • Fukui, M. Guidelines for the diagnosis and treatment of spontaneous occlusion of the circle of Willis ('moyamoya' disease). Research Committee on Spontaneous Occlusion of the Circle of Willis (Moyamoya Disease) of the Ministry of Health and Welfare, Japan. Clin. Neurol. Neurosurg. 99 Suppl 2, S238-240 (1997).
    • (1997) Clin. Neurol. Neurosurg. , vol.99 , pp. S238-S240
    • Fukui, M.1
  • 7
    • 0030722062 scopus 로고    scopus 로고
    • Epidemiological features of moyamoya disease in Japan: Findings from a nationwide survey
    • Wakai, K. et al. Epidemiological features of moyamoya disease in Japan: findings from a nationwide survey. Clin. Neurol. Neurosurg. 99 Suppl 2, S1-5 (1997).
    • (1997) Clin. Neurol. Neurosurg. , vol.99 , pp. S1-S5
    • Wakai, K.1
  • 8
    • 38149058397 scopus 로고    scopus 로고
    • Prevalence and clinicoepidemiological features of moyamoya disease in Japan: Findings from a nationwide epidemiological survey
    • Kuriyama, S. et al. Prevalence and clinicoepidemiological features of moyamoya disease in Japan: findings from a nationwide epidemiological survey. Stroke 39, 42-47, http://dx.doi.org/10.1161/STROKEAHA.107.490714 (2008).
    • (2008) Stroke , vol.39 , pp. 42-47
    • Kuriyama, S.1
  • 9
    • 48249093415 scopus 로고    scopus 로고
    • Novel epidemiological features of moyamoya disease
    • Baba, T., Houkin, K. & Kuroda, S. Novel epidemiological features of moyamoya disease. J. Neurol. Neurosurg. Psychiatry 79, 900-904, http://dx.doi.org/10.1136/jnnp.2007.130666 (2008).
    • (2008) J. Neurol. Neurosurg. Psychiatry , vol.79 , pp. 900-904
    • Baba, T.1    Houkin, K.2    Kuroda, S.3
  • 11
    • 33747411441 scopus 로고    scopus 로고
    • Inheritance pattern of familial moyamoya disease: Autosomal dominant mode and genomic imprinting
    • Mineharu, Y. et al. Inheritance pattern of familial moyamoya disease: autosomal dominant mode and genomic imprinting. J. Neurol. Neurosurg. Psychiatry 77, 1025-1029, http://dx.doi.org/10.1136/jnnp.2006.096040 (2006).
    • (2006) J. Neurol. Neurosurg. Psychiatry , vol.77 , pp. 1025-1029
    • Mineharu, Y.1
  • 12
    • 0006954274 scopus 로고    scopus 로고
    • Linkage of familial moyamoya disease (spontaneous occlusion of the circle of Willis) to chromosome 17q25
    • Yamauchi, T. et al. Linkage of familial moyamoya disease (spontaneous occlusion of the circle of Willis) to chromosome 17q25. Stroke 31, 930-935 (2000).
    • (2000) Stroke , vol.31 , pp. 930-935
    • Yamauchi, T.1
  • 13
    • 84861622356 scopus 로고    scopus 로고
    • Review of past research and current concepts on the etiology of moyamoya disease
    • Houkin, K. et al. Review of past research and current concepts on the etiology of moyamoya disease. Neurol. Med. Chir. (Tokyo). 52, 267-277 (2012).
    • (2012) Neurol. Med. Chir. (Tokyo) , vol.52 , pp. 267-277
    • Houkin, K.1
  • 14
    • 79960608326 scopus 로고    scopus 로고
    • Identification of RNF213 as a susceptibility gene for moyamoya disease and its possible role in vascular development
    • Liu, W. et al. Identification of RNF213 as a susceptibility gene for moyamoya disease and its possible role in vascular development. PLoS One 6, e22542, http://dx.doi.org/10.1371/journal.pone.0022542 (2011).
    • (2011) PLoS One , vol.6 , pp. e22542
    • Liu, W.1
  • 15
    • 79251611133 scopus 로고    scopus 로고
    • A genome-wide association study identifies RNF213 as the first Moyamoya disease gene
    • Kamada, F. et al. A genome-wide association study identifies RNF213 as the first Moyamoya disease gene. J. Hum. Genet. 56, 34-40, http://dx.doi.org/10.1038/jhg.2010.132 (2011).
    • (2011) J. Hum. Genet. , vol.56 , pp. 34-40
    • Kamada, F.1
  • 16
    • 84859929899 scopus 로고    scopus 로고
    • Homozygous c.14576G > A variant of RNF213 predicts earlyonset and severe form of moyamoya disease
    • Miyatake, S. et al. Homozygous c.14576G > A variant of RNF213 predicts earlyonset and severe form of moyamoya disease. Neurology 78, 803-810, http://dx.doi.org/10.1212/WNL.0b013e318249f71f (2012).
    • (2012) Neurology , vol.78 , pp. 803-810
    • Miyatake, S.1
  • 17
    • 84878521797 scopus 로고    scopus 로고
    • P.R4810K, a polymorphism of RNF213, the susceptibility gene for moyamoya disease, is associated with blood pressure
    • Koizumi, A. et al. P.R4810K, a polymorphism of RNF213, the susceptibility gene for moyamoya disease, is associated with blood pressure. Environ Health Prev Med, http://dx.doi.org/10.1007/s12199-012-0299-1 (2012).
    • (2012) Environ Health Prev Med
    • Koizumi, A.1
  • 18
    • 84871514542 scopus 로고    scopus 로고
    • Sibling cases of moyamoya disease having homozygous and heterozygous c.14576G > A variant in RNF213 showed varying clinical course and severity
    • Miyatake, S. et al. Sibling cases of moyamoya disease having homozygous and heterozygous c.14576G > A variant in RNF213 showed varying clinical course and severity. J. Hum. Genet. 57, 804-806, http://dx.doi.org/10.1038/jhg.2012.105 (2012).
    • (2012) J. Hum. Genet. , vol.57 , pp. 804-806
    • Miyatake, S.1
  • 19
    • 84867861292 scopus 로고    scopus 로고
    • Molecular analysis of RNF213 gene for moyamoya disease in the Chinese Han population
    • Wu, Z. et al. Molecular analysis of RNF213 gene for moyamoya disease in the Chinese Han population. PLoS One 7, e48179, http://dx.doi.org/10.1371/journal.pone.0048179 (2012).
    • (2012) PLoS One , vol.7 , pp. e48179
    • Wu, Z.1
  • 20
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D. D., Wolf, Y. I., Koonin, E. V. & Aravind, L. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317, 41-72, http://dx.doi.org/ 10.1006/jmbi.2001.5378 (2002).
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 21
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • Hershko, A. & Ciechanover, A. The ubiquitin system. Annu. Rev. Biochem. 67, 425-479, http://dx.doi.org/10.1146/annurev.biochem.67.1.425 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 22
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro, C. A. &Weissman, A. M. RING finger proteins: mediators of ubiquitin ligase activity. Cell 102, 549-552 (2000).
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 23
    • 0034885052 scopus 로고    scopus 로고
    • AAA1 superfamily ATPases: Common structure - Diverse function
    • Ogura, T. & Wilkinson, A. J. AAA1 superfamily ATPases: common structure - diverse function. Genes Cells 6, 575-597 (2001).
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 24
    • 21744446127 scopus 로고    scopus 로고
    • AAA1 proteins: Have engine, will work
    • Hanson, P. I.&Whiteheart, S. W. AAA1 proteins: have engine, will work. Nat Rev Mol Cell Biol 6, 519-529, http://dx.doi.org/10.1038/nrm1684 (2005).
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 519-529
    • Hanson, P.I.1    Whiteheart, S.W.2
  • 25
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J. R. & Lindquist, S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82 (1998).
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 26
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state
    • Lee, S. et al. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 115, 229-240 (2003).
    • (2003) Cell , vol.115 , pp. 229-240
    • Lee, S.1
  • 27
    • 0036238432 scopus 로고    scopus 로고
    • Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein
    • Cashikar, A. G. et al. Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol. Cell 9, 751-760 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 751-760
    • Cashikar, A.G.1
  • 28
    • 84870831488 scopus 로고    scopus 로고
    • A tightly regulated molecular toggle controls AAA+ disaggregase
    • Oguchi, Y. et al. A tightly regulated molecular toggle controls AAA+ disaggregase. Nat Struct Mol Biol 19, 1338-1346, http://dx.doi.org/10.1038/nsmb.2441 (2012).
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1338-1346
    • Oguchi, Y.1
  • 29
    • 84870792675 scopus 로고    scopus 로고
    • Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
    • Seyffer, F. et al. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat Struct Mol Biol 19, 1347-1355, http://dx.doi.org/10.1038/nsmb.2442 (2012).
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1347-1355
    • Seyffer, F.1
  • 30
    • 0029645318 scopus 로고
    • The 70S Escherichia coli ribosome at 23 A resolution: Fitting the ribosomal RNA
    • Stark, H. et al. The 70S Escherichia coli ribosome at 23 A resolution: fitting the ribosomal RNA. Structure 3, 815-821 (1995).
    • (1995) Structure , vol.3 , pp. 815-821
    • Stark, H.1
  • 32
    • 33751229633 scopus 로고    scopus 로고
    • Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs
    • Pack, C., Saito, K., Tamura, M. & Kinjo, M. Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs. Biophys. J. 91, 3921-3936, http://dx.doi.org/10.1529/biophysj.105.079467 (2006).
    • (2006) Biophys. J. , vol.91 , pp. 3921-3936
    • Pack, C.1    Saito, K.2    Tamura, M.3    Kinjo, M.4
  • 33
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell, D. A., Kowal, A. S. & Lindquist, S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J. Biol. Chem. 269, 4480-4487 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 34
    • 0033595814 scopus 로고    scopus 로고
    • Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
    • Hartman, J. J. & Vale, R. D. Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science 286, 782-785 (1999).
    • (1999) Science , vol.286 , pp. 782-785
    • Hartman, J.J.1    Vale, R.D.2
  • 35
    • 0037427531 scopus 로고    scopus 로고
    • Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities
    • Wang, Q., Song, C. & Li, C. C. Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities. Biochem. Biophys. Res. Commun. 300, 253-260 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 253-260
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 36
    • 0037705402 scopus 로고    scopus 로고
    • Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity
    • Mogk, A. et al. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J. Biol. Chem. 278, 17615-17624, http://dx.doi.org/10.1074/jbc.M209686200 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 17615-17624
    • Mogk, A.1
  • 37
    • 0032969563 scopus 로고    scopus 로고
    • AAA1: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L. & Koonin, E. V. AAA1: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (1999).
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 39
    • 77949425813 scopus 로고    scopus 로고
    • Assembly of the AAA ATPase Vps4 on ESCRT-III
    • Shestakova, A. et al. Assembly of the AAA ATPase Vps4 on ESCRT-III. Mol. Biol. Cell 21, 1059-1071, http://dx.doi.org/10.1091/mbc.E09-07-0572 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1059-1071
    • Shestakova, A.1
  • 40
    • 33644525938 scopus 로고    scopus 로고
    • Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1
    • Azmi, I. et al. Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. J. Cell Biol. 172, 705-717, http://dx.doi.org/10.1083/jcb.200508166 (2006).
    • (2006) J. Cell Biol. , vol.172 , pp. 705-717
    • Azmi, I.1
  • 41
    • 33645741669 scopus 로고    scopus 로고
    • Adaptor protein controlled oligomerization activates the AAA+ protein ClpC
    • Kirstein, J. et al. Adaptor protein controlled oligomerization activates the AAA+ protein ClpC. EMBO J. 25, 1481-1491, http://dx.doi.org/10.1038/sj.emboj. 7601042 (2006).
    • (2006) EMBO J. , vol.25 , pp. 1481-1491
    • Kirstein, J.1
  • 42
    • 0037250367 scopus 로고    scopus 로고
    • Enlarged FAMSBASE: Protein 3D structure models of genome sequences for 41 species
    • Yamaguchi, A. et al. Enlarged FAMSBASE: protein 3D structure models of genome sequences for 41 species. Nucleic Acids Res 31, 463-468 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 463-468
    • Yamaguchi, A.1
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55, 29-32 (1996).
    • (1996) J. Mol. Graph. , vol.14
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 44
    • 0022549284 scopus 로고
    • A direct colorimetric assay for Ca2+ -stimulated ATPase activity
    • Chan, K. M., Delfert, D. & Junger, K. D. A direct colorimetric assay for Ca2+ -stimulated ATPase activity. Anal. Biochem. 157, 375-380 (1986).
    • (1986) Anal. Biochem. , vol.157 , pp. 375-380
    • Chan, K.M.1    Delfert, D.2    Junger, K.D.3
  • 45
    • 44949249968 scopus 로고    scopus 로고
    • Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508
    • Morito, D. et al. Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508. Mol. Biol. Cell 19, 1328-1336, http://dx.doi.org/10.1091/mbc.E07-06-0601 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1328-1336
    • Morito, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.