title: NIP-SNAP-1 and -2 mitochondrial proteins are maintained by heat shock protein 60.
abstract: NIP-SNAP-1 and -2 are ubiquitous proteins thought to be associated with maintenance of mitochondrial function, neuronal transmission, and autophagy. However, their physiological functions remain largely unknown. To elucidate their functional importance, we screened for proteins that interact with NIP-SNAP-1 and -2, resulting in identification of HSP60 and P62/SQSTM1 as binding proteins. NIP-SNAP-1 and -2 localized in the mitochondrial inner membrane space, whereas HSP60 localized in the matrix. Native gel electrophoresis and filter trap assays revealed that human HSP60 prevented aggregation of newly synthesized NIP-SNAP-2 in an in vitro translation system. Moreover, expression levels of NIP-SNAP-1 and -2 in cells were decreased by knockdown of HSP60, but not HSP10. These findings indicate that HSP60 promotes folding and maintains the stability of NIP-SNAP-1 and -2.
authors.affiliation: Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Soh
authors.initials: S
authors.lastname: Yamamoto
authors.affiliation: Department of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, Japan.
authors.forename: Tomoya
authors.initials: T
authors.lastname: Okamoto
authors.affiliation: Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan; Department of Otorhinolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Noriko
authors.initials: N
authors.lastname: Ogasawara
authors.affiliation: Department of Pediatrics, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Shin
authors.initials: S
authors.lastname: Hashimoto
authors.affiliation: Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Tsukasa
authors.initials: T
authors.lastname: Shiraishi
authors.affiliation: Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Toyotaka
authors.initials: T
authors.lastname: Sato
authors.affiliation: Department of Otorhinolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Keisuke
authors.initials: K
authors.lastname: Yamamoto
authors.affiliation: Department of Pediatrics, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Tsutsumi
authors.affiliation: Department of Otorhinolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Kenichi
authors.initials: K
authors.lastname: Takano
authors.affiliation: Department of Otorhinolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.
authors.forename: Testuo
authors.initials: T
authors.lastname: Himi
authors.affiliation: Department of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, Japan.
authors.forename: Hideaki
authors.initials: H
authors.lastname: Itoh
authors.affiliation: Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan. Electronic address: syokota@sapmed.ac.jp.
authors.forename: Shin-Ichi
authors.initials: SI
authors.lastname: Yokota
mesh_terms: D002460:Cell Line; D018835:Chaperonin 10 / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D018834:Chaperonin 60 / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D055785:Gene Knockdown Techniques; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051336:Mitochondrial Membranes / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010750:Phosphoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D060066:Protein Interaction Maps; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000071456:Sequestosome-1 Protein / Q000378:metabolism
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; C060293:HSPD1 protein, human; D036341:Intercellular Signaling Peptides and Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; C113197:NIPSNAP1 protein, human; C113390:NIPSNAP2 protein, human; D010750:Phosphoproteins; D011506:Proteins; D011994:Recombinant Proteins; C099718:SQSTM1 protein, human; D000071456:Sequestosome-1 Protein
keywords: HSP60; Mitochondria; NIP-SNAP; Protein folding; Protein-protein interaction