Faculty Profiles - SHIBATA, Hideki

Papers - SHIBATA, Hideki

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The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins. Reviewed International journal Open Access

Terunao Takahara, Kuniko Inoue, Yumika Arai, Keiko Kuwata, Hideki Shibata, Masatoshi Maki

The Journal of biological chemistry Vol. 292 ( 41 ) page： 17057 - 17072 2017.10

Language：English Publishing type：Research paper (scientific journal)

Mobilization of intracellular calcium is essential for a wide range of cellular processes, including signal transduction, apoptosis, and vesicular trafficking. Several lines of evidence have suggested that apoptosis-linked gene 2 (ALG-2, also known as PDCD6), a calcium-binding protein, acts as a calcium sensor linking calcium levels with efficient vesicular trafficking, especially at the endoplasmic reticulum (ER)-to-Golgi transport step. However, how ALG-2 regulates these processes remains largely unclear. Here, we report that MAPK1-interacting and spindle-stabilizing (MISS)-like (MISSL), a previously uncharacterized protein, interacts with ALG-2 in a calcium-dependent manner. Live-cell imaging revealed that upon a rise in intracellular calcium levels, GFP-tagged MISSL (GFP-MISSL) dynamically relocalizes in a punctate pattern and colocalizes with ALG-2. MISSL knockdown caused disorganization of the components of the ER exit site, the ER-Golgi intermediate compartment, and Golgi. Importantly, knockdown of either MISSL or ALG-2 attenuated the secretion of secreted alkaline phosphatase (SEAP), a model secreted cargo protein, with similar reductions in secretion by single- and double-protein knockdowns, suggesting that MISSL and ALG-2 act in the same pathway to regulate the secretion process. Furthermore, ALG-2 or MISSL knockdown delayed ER-to-Golgi transport of procollagen type I. We also found that ALG-2 and MISSL interact with microtubule-associated protein 1B (MAP1B) and that MAP1B knockdown reverts the reduced secretion of SEAP caused by MISSL or ALG-2 depletion. These results suggest that a change in the intracellular calcium level plays a role in regulation of the secretory pathway via interaction of ALG-2 with MISSL and MAP1B.

DOI： 10.1074/jbc.M117.800201

Web of Science

Scopus

PubMed

Mutations in the vesicular trafficking protein annexin A11 are associated with amyotrophic lateral sclerosis Reviewed Open Access

Bradley N. Smith, Simon D. Topp, Claudia Fallini, Hideki Shibata, Han-Jou Chen, Claire Troakes, Andrew King, Nicola Ticozzi, Kevin P. Kenna, Athina Soragia-Gkazi, Jack W. Miller, Akane Sato, Diana Marques Dias, Maryangel Jeon, Caroline Vance, Chun Hao Wong, Martina de Majo, Wejdan Kattuah, Jacqueline C. Mitchell, Emma L. Scotter, Nicholas W. Parkin, Peter C. Sapp, Matthew Nolan, Peter J. Nestor, Michael Simpson, Michael Weale, Monkel Lek, Frank Baas, J. M. Vianney de Jong, Anneloor L. M. A. ten Asbroek, Alberto Garcia Redondo, Jesus Esteban-Perez, Cinzia Tiloca, Federico Verde, Stefano Duga, Nigel Leigh, Hardev Pall, Karen E. Morrison, Ammar Al-Chalabi, Pamela J. Shaw, Janine Kirby, Martin R. Turner, Kevin Talbot, Orla Hardiman, Jonathan D. Glass, Jacqueline de Belleroche, Masatoshi Maki, Stephen E. Moss, Christopher Miller, Cinzia Gellera, Antonia Ratti, Safa Al-Sarraj, Robert H. Brown, Vincenzo Silani, John E. Landers, Christopher E. Shaw

SCIENCE TRANSLATIONAL MEDICINE Vol. 9 ( 388 ) page： eaad9157 2017.5

Language：English Publishing type：Research paper (scientific journal) Publisher：AMER ASSOC ADVANCEMENT SCIENCE

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder. We screened 751 familial ALS patient whole-exome sequences and identified six mutations including p.D40G in the ANXA11 gene in 13 individuals. The p.D40G mutation was absent from 70,000 control whole-exome sequences. This mutation segregated with disease in two kindreds and was present in another two unrelated cases (P = 0.0102), and all mutation carriers shared a common founder haplotype. Annexin A11-positive protein aggregates were abundant in spinal cord motor neurons and hippocampal neuronal axons in an ALS patient carrying the p.D40G mutation. Transfected human embryonic kidney cells expressing ANXA11 with the p.D40G mutation and other N-terminal mutations showed altered binding to calcyclin, and the p.R235Q mutant protein formed insoluble aggregates. We conclude that mutations in ANXA11 are associated with ALS and implicate defective intracellular protein trafficking in disease pathogenesis.

DOI： 10.1126/scitranslmed.aad9157

Web of Science

Scopus

PubMed

The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein. Reviewed International journal Open Access

Takashi Kanadome, Hideki Shibata, Keiko Kuwata, Terunao Takahara, Masatoshi Maki

The FEBS journal Vol. 284 ( 1 ) page： 56 - 76 2017.1

Language：English Publishing type：Research paper (scientific journal)

Apoptosis-linked gene 2 (ALG-2), which is a gene product of PDCD6, is a 22-kDa Ca2+ -binding protein. Accumulating evidence points to a role for ALG-2 as a Ca2+ -responsive adaptor protein. On binding to Ca2+ , ALG-2 undergoes a conformational change that facilitates its interaction with various proteins. It also forms a homodimer and heterodimer with peflin, a paralog of ALG-2. However, the differences in cellular roles for the ALG-2 homodimer and ALG-2/peflin heterodimer are unclear. In the present study, we found that Trk-fused gene (TFG) protein interacted with the ALG-2 homodimer. Immunostaining analysis revealed that TFG and ALG-2 partially overlapped at endoplasmic reticulum exit sites (ERES), a platform for COPII-mediated protein transport from the endoplasmic reticulum. Time-lapse live-cell imaging demonstrated that both green fluorescent protein-fused TFG and mCherry-fused ALG-2 are recruited to ERES after thapsigargin treatment, which raises intracellular Ca2+ levels. Furthermore, overexpression of ALG-2 induced the accumulation of TFG at ERES. TFG has an ALG-2-binding motif and deletion of the motif decreased TFG binding to ALG-2 and shortened its half-life at ERES, suggesting a critical role for ALG-2 in retaining TFG at ERES. We also demonstrated, by in vitro cross-linking assays, that ALG-2 promoted the polymerization of TFG in a Ca2+ -dependent manner. Collectively, the results suggest that ALG-2 acts as a Ca2+ -sensitive adaptor to concentrate and polymerize TFG at ERES, supporting a potential role for ALG-2 in COPII-dependent trafficking from the endoplasmic reticulum.

DOI： 10.1111/febs.13949

Web of Science

Scopus

PubMed

Multifaceted Roles of ALG-2 in Ca²⁺-Regulated Membrane Trafficking. Reviewed

Masatoshi Maki, Terunao Takahara, Hideki Shibata

International Journal of Molecular Sciences Vol. 17 ( 9 ) page： E1401 2016.8

Tubby-like protein superfamily member PLSCR3 functions as a negative regulator of adipogenesis in mouse 3T3-L1 preadipocytes by suppressing induction of late differentiation stage transcription factors. Reviewed

Akira Inokawa, Tatsutoshi Inuzuka, Terunao Takahara, Hideki Shibata, Masatoshi Maki

Bioscience Reports Vol. 36 ( 1 ) page： e00287 2016.1

A New Role for Annexin A11 in the Early Secretory Pathway via Stabilizing Sec31A Protein at the Endoplasmic Reticulum Exit Sites (ERES). Reviewed

Hideki Shibata, Takashi Kanadome, Hirofumi Sugiura, Takeru Yokoyama, Minami Yamamuro, Stephen E. Moss, Masatoshi Maki

The Journal of Biological Chemistry Vol. 290 ( 8 ) page： 4981-4993 2015.2

Structural Analysis of the Complex between Penta-EF-Hand ALG-2 Protein and Sec31A Peptide Reveals a Novel Target Recognition Mechanism of ALG-2 Reviewed

Takeshi Takahashi, Kyosuke Kojima, Wei Zhang, Kanae Sasaki, Masaru Ito, Hironori Suzuki, Masato Kawasaki, Soichi Wakatsuki, Terunao Takahara, Hideki Shibata, Masatoshi Maki

International Journal of Molecular Sciences Vol. 16 ( 2 ) page： 3677-3699 2015.2

Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway. Reviewed

Yuki Maemoto, Yasuko Ono, Satomi Kiso, Hideki Shibata, Terunao Takahara, Hiroyuki Sorimachi, Masatoshi Maki

FEBS J. Vol. 281 ( 16 ) page： 3642-3655 2014.7

Nuclear ALG-2 protein interacts with Ca2+ homeostasis endoplasmic reticulum protein (CHERP) Ca2+-dependently and participates in regulation of alternative splicing of inositol trisphosphate receptor type 1 (IP3R1) pre-mRNA. Reviewed

Kanae Sasaki-Osugi, Chiaki Imoto, Terunao Takahara, Hideki Shibata, Masatoshi Maki

J. Biol. Chem. Vol. 288 ( 46 ) page： 33361-33375 2013.9

VPS37 isoforms differentially modulate the ternary complex formation of ALIX, ALG-2, and ESCRT-I. Reviewed

Mayumi Okumura, Angela M. Katsuyama, Hideki Shibata, Masatoshi Maki

Biosci. Biotechnol. Biochem. Vol. 77 ( 8 ) page： 1715-1721 2013.8

Identification of phosphorylation sites in the C-terminal region of charged multivesicular body protein 1A (CHMP1A). Reviewed

Yuki Maemoto, Hideki Shibata, Masatoshi Maki

Biosci. Biotechnol. Biochem. Vol. 77 ( 6 ) page： 1317-1319 2013.6

Mammalian ESCRT-III-related protein IST1 has a distinctive Met-Pro repeat sequence that is essential for interaction with ALG-2 in the presence of Ca2+. Reviewed

Mayumi Okumura, Takeshi Takahashi, Hideki Shibata, Masatoshi Maki

Biosci. Biotechnol. Biochem. Vol. 77 ( 5 ) page： 1049-1054 2013.5

Analysis of limited proteolytic activity of calpain-7 using non-physiological substrates in mammalian cells. Reviewed

Yuki Maemoto, Satomi Kiso, Hideki Shibata, Masatoshi Maki

FEBS J. Vol. 280 ( 11 ) page： 2594-2607 2013.4

ALG-2-interacting Tubby-like protein superfamily member PLSCR3 is secreted by an exosomal pathway and taken up by recipient cultured cells. Reviewed

Tatsutoshi Inuzuka, Akira Inokawa, Cen Chen, Kumiko Kizu, Hiroshi Narita, Hideki Shibata, Masatoshi Maki

Biosci. Rep. Vol. 33 ( 2 ) page： e00026 2013.3

Biochemical and immunological detection of physical interactions between penta-EF-hand protein ALG-2 and its binding partners. Reviewed

Kanae Osugi, Hideki Shibata, Masatoshi Maki

Methods Mol Biol. Vol. 963 page： 187-200 2012.11

Prediction of a New Ligand-Binding Site for Type 2 Motif based on the Crystal Structure of ALG-2 by Dry and Wet Approaches. Reviewed

Takeshi Takahashi, Hironori Suzuki, Tatsutoshi Inuzuka, Hideki Shibata, Masatoshi Maki

Int J Mol Sci. Vol. 13 ( 6 ) page： 7535-7549 2012.6

Identification of the P-body component PATL1 as a novel ALG-2-interacting protein by in silico and far-Western screening of proline-rich proteins. Reviewed

Kanae Osugi, Hironori Suzuki, Tomomi Nomura, Yasuo Ariumi, Hideki Shibata, Masatoshi Maki

J Biochem. Vol. 151 ( 6 ) page： 657-666 2012.6

Evolutionary and physical linkage between calpains and penta-EF-hand Ca2+-binding proteins. Reviewed

Masatoshi Maki, Yuki Maemoto, Yohei Osako, Hideki Shibata

FEBS J. Vol. 279 ( 8 ) page： 1414-1421 2012.4

Calpain-7 binds to CHMP1B at its second α-helical region and forms a ternary complex with IST1. Reviewed

Yuki Maemoto, Yohei Osako, Emi Goto, Eri Nozawa, Hideki Shibata, Masatoshi Maki

J. Biochem. Vol. 150 ( 4 ) page： 411-421 2011.10

Structure and function of ALG-2, a penta-EF-hand calcium-dependent adaptor protein. Reviewed

Masatoshi Maki, Hironori Suzuki, Hideki Shibata

Sci China Life Sci. Vol. 54 ( 8 ) page： 770-779 2011.8

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Papers - SHIBATA, Hideki