JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mizutani, A.
Right arrow Articles by Mikoshiba, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mizutani, A.
Right arrow Articles by Mikoshiba, K.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 13, 9823-9831, March 31, 2000

SYNCRIP, a Cytoplasmic Counterpart of Heterogeneous Nuclear Ribonucleoprotein R, Interacts with Ubiquitous Synaptotagmin Isoforms*

Akihiro MizutaniDagger §, Mitsunori FukudaDagger , Keiji IbataDagger , Yoko Shiraishi||, and Katsuhiko MikoshibaDagger **

From the Laboratory for Dagger  Developmental Neurobiology and for || Molecular Neurogenesis, the Brain Science Institute, the Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0198, the  Department of Molecular Neurobiology, the Institute of Medical Science, the University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, and the ** Calciosignal Net Project, Exploratory Research for Advanced Technology, Japan Science and Technology Corporation, 2-28-8 Honkomagome, Bunkyo-ku, Tokyo 113-0021, Japan

Synaptotagmins (Syts) are a large family of membrane proteins consisted of at least 12 isoforms. They are categorized in neuron-specific isoforms (I-V, X, and XI) and ubiquitous isoforms (VI-IX) based on their expression patterns. Syt-I, a neuron-specific and abundant isoform, has been well characterized and postulated to be the exocytotic Ca2+ sensor. However, the functions of other isoforms remain obscure. Here, we report that ubiquitous isoforms of synaptotagmins, Syt-VII, Syt-VIII, and Syt-IX, interacted with a cytoplasmic RNA-binding protein, SYNCRIP (Synaptotagmin-binding, cytoplasmic RNA-interacting protein), through their C2B domains. SYNCRIP was originally found in the Syt-II C2AB domain bound fraction from the mouse brain lysate. cDNA cloning of SYNCRIP cDNA revealed that the protein was highly homologous to heterogeneous nuclear ribonucleoprotein R (hnRNP R) recently identified. SYNCRIP protein was ubiquitously and constantly expressed in various tissues of mice parallel to hnRNP R. SYNCRIP indeed bound RNA with preference to poly(A) RNA; however, in contrast to the nuclear localization of hnRNP R, SYNCRIP was distributed predominantly in the cytoplasm as judged by both biochemical fractionation and immunohistochemical studies. In vitro binding experiments showed the potential interaction of SYNCRIP with C2B domains of Syts except for those of Syt-V, -VI, and -X. Furthermore, the interaction between SYNCRIP and Syt-VII, -VIII, or -IX was revealed by co-immunoprecipitation experiments using COS cells transiently expressing each Syt isoform. These findings suggested that SYNCRIP was a target of ubiquitous type of Syts and implied the involvement of ubiquitous Syts in the regulation of dynamics of the cytoplasmic mRNA.

* This work was supported in part by grants from the Science and Technology Agency of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB035725.

§ To whom correspondence should be addressed: Developmental Neurobiology Laboratory, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Tel.: 81-48-467-9745; Fax: 81-48-467-9744; E-mail: amizutan@ims.u-tokyo.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Genes Dev.Home page
T.-D. Kim, K.-C. Woo, S. Cho, D.-C. Ha, S. K. Jang, and K.-T. Kim
Rhythmic control of AANAT translation by hnRNP Q in circadian melatonin production
Genes & Dev., April 1, 2007; 21(7): 797 - 810.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
S. Cho, S. M. Park, T. D. Kim, J. H. Kim, K.-T. Kim, and S. K. Jang
BiP Internal Ribosomal Entry Site Activity Is Controlled by Heat-Induced Interaction of NSAP1
Mol. Cell. Biol., January 1, 2007; 27(1): 368 - 383.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
G. Elvira, S. Wasiak, V. Blandford, X.-K. Tong, A. Serrano, X. Fan, M. del Rayo Sanchez-Carbente, F. Servant, A. W. Bell, D. Boismenu, et al.
Characterization of an RNA Granule from Developing Brain
Mol. Cell. Proteomics, April 1, 2006; 5(4): 635 - 651.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
T.-D. Kim, J.-S. Kim, J. H. Kim, J. Myung, H.-D. Chae, K.-C. Woo, S. K. Jang, D.-S. Koh, and K.-T. Kim
Rhythmic Serotonin N-Acetyltransferase mRNA Degradation Is Essential for the Maintenance of Its Circadian Oscillation
Mol. Cell. Biol., April 15, 2005; 25(8): 3232 - 3246.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Angenstein, A. M. Evans, S.-C. Ling, R. E. Settlage, S. Ficarro, F. A. Carrero-Martinez, J. Shabanowitz, D. F. Hunt, and W. T. Greenough
Proteomic Characterization of Messenger Ribonucleoprotein Complexes Bound to Nontranslated or Translated Poly(A) mRNAs in the Rat Cerebral Cortex
J. Biol. Chem., February 25, 2005; 280(8): 6496 - 6503.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Bannai, K. Fukatsu, A. Mizutani, T. Natsume, S.-i. Iemura, T. Ikegami, T. Inoue, and K. Mikoshiba
An RNA-interacting Protein, SYNCRIP (Heterogeneous Nuclear Ribonuclear Protein Q1/NSAP1) Is a Component of mRNA Granule Transported with Inositol 1,4,5-Trisphosphate Receptor Type 1 mRNA in Neuronal Dendrites
J. Biol. Chem., December 17, 2004; 279(51): 53427 - 53434.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
K. S. Choi, A. Mizutani, and M. M. C. Lai
SYNCRIP, a Member of the Heterogeneous Nuclear Ribonucleoprotein Family, Is Involved in Mouse Hepatitis Virus RNA Synthesis
J. Virol., December 1, 2004; 78(23): 13153 - 13162.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
J. H. Kim, K. Y. Paek, S. H. Ha, S. Cho, K. Choi, C. S. Kim, S. H. Ryu, and S. K. Jang
A Cellular RNA-Binding Protein Enhances Internal Ribosomal Entry Site-Dependent Translation through an Interaction Downstream of the Hepatitis C Virus Polyprotein Initiation Codon
Mol. Cell. Biol., September 15, 2004; 24(18): 7878 - 7890.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Ibarrola, H. Molina, A. Iwahori, and A. Pandey
A Novel Proteomic Approach for Specific Identification of Tyrosine Kinase Substrates Using [13C]Tyrosine
J. Biol. Chem., April 16, 2004; 279(16): 15805 - 15813.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
S. M. Carty and A. L. Greenleaf
Hyperphosphorylated C-terminal Repeat Domain-associating Proteins in the Nuclear Proteome Link Transcription to DNA/Chromatin Modification and RNA Processing
Mol. Cell. Proteomics, August 1, 2002; 1(8): 598 - 610.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. C. Hresko and M. Mueckler
Identification of pp68 as the Tyrosine-phosphorylated Form of SYNCRIP/NSAP1. A CYTOPLASMIC RNA-BINDING PROTEIN
J. Biol. Chem., July 5, 2002; 277(28): 25233 - 25238.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
W. Rossoll, A.-K. Kroning, U.-M. Ohndorf, C. Steegborn, S. Jablonka, and M. Sendtner
Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing in motor axons?
Hum. Mol. Genet., January 1, 2002; 11(1): 93 - 105.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Fukuda, C. Saegusa, E. Kanno, and K. Mikoshiba
The C2A Domain of Double C2 Protein gamma Contains a Functional Nuclear Localization Signal
J. Biol. Chem., June 29, 2001; 276(27): 24441 - 24444.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.