NIP-SNAP-1 and -2 mitochondrial proteins are maintained by heat shock protein 60

Soh Yamamoto; Tomoya Okamoto; Noriko Ogasawara; Shin Hashimoto; Tsukasa Shiraishi; Toyotaka Sato; Keisuke Yamamoto; Hiroyuki Tsutsumi; Kenichi Takano; Testuo Himi; Hideaki Itoh; Shin-Ichi Yokota

doi:10.1016/j.bbrc.2016.12.133

NIP-SNAP-1 and -2 mitochondrial proteins are maintained by heat shock protein 60

Biochem Biophys Res Commun. 2017 Feb 12;483(3):917-922. doi: 10.1016/j.bbrc.2016.12.133. Epub 2016 Dec 21.

Authors

Affiliations

¹ Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan.
² Department of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, Japan.
³ Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan; Department of Otorhinolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.
⁴ Department of Pediatrics, Sapporo Medical University School of Medicine, Sapporo, Japan.
⁵ Department of Otorhinolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.
⁶ Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan. Electronic address: syokota@sapmed.ac.jp.

PMID: 28011268
DOI: 10.1016/j.bbrc.2016.12.133

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.

Keywords: HSP60; Mitochondria; NIP-SNAP; Protein folding; Protein-protein interaction.

MeSH terms

Cell Line
Chaperonin 10 / antagonists & inhibitors
Chaperonin 10 / genetics
Chaperonin 10 / metabolism
Chaperonin 60 / antagonists & inhibitors
Chaperonin 60 / genetics
Chaperonin 60 / metabolism*
Gene Knockdown Techniques
Humans
Intercellular Signaling Peptides and Proteins
Intracellular Signaling Peptides and Proteins
Membrane Proteins / chemistry
Membrane Proteins / genetics
Membrane Proteins / metabolism*
Mitochondrial Membranes / metabolism
Mitochondrial Proteins / antagonists & inhibitors
Mitochondrial Proteins / chemistry
Mitochondrial Proteins / genetics
Mitochondrial Proteins / metabolism*
Phosphoproteins / chemistry
Phosphoproteins / genetics
Phosphoproteins / metabolism*
Protein Binding
Protein Folding
Protein Interaction Maps
Protein Stability
Proteins / chemistry
Proteins / genetics
Proteins / metabolism*
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / metabolism
Sequestosome-1 Protein / metabolism

Substances

Chaperonin 10
Chaperonin 60
HSPD1 protein, human
Intercellular Signaling Peptides and Proteins
Intracellular Signaling Peptides and Proteins
Membrane Proteins
Mitochondrial Proteins
NIPSNAP1 protein, human
NIPSNAP2 protein, human
Phosphoproteins
Proteins
Recombinant Proteins
SQSTM1 protein, human
Sequestosome-1 Protein