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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
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Related Experiment Video

Updated: May 8, 2026

Imaging Initial Ca2+ Microdomains in Primary T Cells
05:56

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Published on: October 4, 2024

The C2B domain is the primary Ca2+ sensor in DOC2B: a structural and functional analysis.

Moshe Giladi1, Lirin Michaeli, Lior Almagor

  • 1Department of Physiology and Pharmacology, Sackler School of Medicine, Tel-Aviv University, Ramat-Aviv 69978, Israel.

Journal of Molecular Biology
|September 3, 2013
PubMed
Summary

The double-C2 domain (DOC2B) protein acts as a calcium (Ca2+) sensor in neurotransmitter release. Researchers found the C2B domain is the primary Ca2+ sensor, while C2A enhances plasma membrane interaction.

Keywords:
ASAC(2) domainDESYDOC2BDeutsches Elektronen SynchrotronEDTAEOMMDPLPMSAXSSNAREULVX-ray crystallography[Ca2+](i)accessible surface areaensemble optimization methodethylenediaminetetraacetic acidexocytosisintracellular calciummolecular dynamicsphospholipidplasma membranesmall-angle X-ray scatteringsoluble NSF attachment receptorsynaptic transmissionunilamellar vesicle

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Last Updated: May 8, 2026

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • DOC2B protein functions as a high-affinity calcium (Ca2+) sensor.
  • It plays a role in spontaneous and asynchronous neurotransmitter release.

Purpose of the Study:

  • To determine the molecular features of DOC2B's Ca2+ sensing capabilities.
  • To elucidate the structure-function relationships of its C2A and C2B domains.

Main Methods:

  • Crystal structure determination of C2A and C2B domains.
  • Small-angle X-ray scattering (SAXS) for C2AB solution structure.
  • Live cell imaging and kinetic studies.

Main Results:

  • C2B domain exhibits significantly higher Ca2+ binding affinity than C2A.
  • The C2AB tandem domain structure is flexible, with Ca2+ binding stabilizing interaction with vesicles.
  • C2B translocates to the plasma membrane (PM) at 400 nM Ca2+; C2A does not.
  • C2AB shows enhanced PM translocation compared to C2B alone.

Conclusions:

  • The C2B domain is the principal Ca2+ sensing component of DOC2B.
  • The C2A domain modulates DOC2B's interaction with the plasma membrane.
  • Structural and functional studies reveal domain-specific roles in Ca2+ sensing and membrane targeting.