FEBS Letters
Volume 583, Issue 18 , Pages 3050-3056, 17 September 2009

Pleiotropic roles of calumenin (calu-1), a calcium-binding ER luminal protein, in Caenorhabditis elegans

Edited by Ned Mantei

  • Jeong Hoon Cho

      Affiliations

    • Division of Biology Education, College of Education, Chosun University, Gwangju 501-759, Republic of Korea
    • These authors contributed equally to this work.
  • ,
  • Hyun-Ok Song

      Affiliations

    • Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea
    • These authors contributed equally to this work.
  • ,
  • Gunasekaran Singaravelu

      Affiliations

    • Department of Life Science, BK21 (Life Science for Global Warming Team), College of Natural Sciences, Hanyang University, Seoul 133-791, Republic of Korea
    • Present address: Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA.
  • ,
  • Hyun Sung

      Affiliations

    • Department of Life Science, BK21 (Life Science for Global Warming Team), College of Natural Sciences, Hanyang University, Seoul 133-791, Republic of Korea
  • ,
  • Won-Chan Oh

      Affiliations

    • Department of Life Science, BK21 (Life Science for Global Warming Team), College of Natural Sciences, Hanyang University, Seoul 133-791, Republic of Korea
    • Present address: Cell and Developmental Biology, University of California Davis, Davis, CA 95616, USA.
  • ,
  • Soonjae Kwon

      Affiliations

    • Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea
  • ,
  • Do Han Kim

      Affiliations

    • Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea
  • ,
  • Joohong Ahnn

      Affiliations

    • Department of Life Science, BK21 (Life Science for Global Warming Team), College of Natural Sciences, Hanyang University, Seoul 133-791, Republic of Korea
    • Corresponding Author InformationCorresponding author. Fax: +82 2 2220 4474.

Received 19 May 2009; received in revised form 11 August 2009; accepted 13 August 2009. published online 18 August 2009.

Abstract 

Calumenin is a Ca2+ binding protein localizing at the lumen of the endoplasmic reticulum (ER). Although it has been implicated in various diseases, the in vivo functions of calumenin are largely unknown. Here, we report that calumenin has pleiotropic roles in muscle and cuticle function in Caenorhabditis elegans. Mutant analysis revealed that the calu-1 is required for regulating fertility, locomotion and body size. In addition, calu-1 is important for two behaviors, defecation and pharyngeal pumping, consistent with its ability to bind Ca2+. The genetic analysis further suggested the possibility that calu-1 regulates the pharyngeal pumping together with the inositol 1,4,5-triphosphate (IP3) receptor encoded by itr-1. Taken together, our data suggest that calumenin is important for calcium signaling pathways in C. elegans.

Abbreviations: ER, endoplasmic reticulum, IPTG, isopropyl β-d-1-thiogalactopyranoside, SERCA, sarcoplasmic reticulum Ca2+-transporting ATPase, HIV, human immunodeficiency virus, pBoc, posterior body contraction, SEM, scanning electron microscopy, RNAi, RNA interference, IP3, inositol 1,4,5-triphosphate, PDI, protein disulfide isomerase, PPIase, peptidyl prolyl cis–trans isomerase

Keywords: Ca2+ signaling, EF hand, Defecation, Pharyngeal pumping, Cuticle defect

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(09)00635-8

doi:10.1016/j.febslet.2009.08.018

FEBS Letters
Volume 583, Issue 18 , Pages 3050-3056, 17 September 2009