Annexin A2 expression and partners during epithelial cell differentiation.
Malik Zibouche1,1, Françoise Illien1,1, Jesus Ayala-Sanmartin1,1
1CNRS, Université Sorbonne, École normale supérieure, Université PSL, Laboratoire des biomolécules, Paris 75005, France.
Summary
Annexin A2 partners with E-cadherin, actin, and caveolin 1 during epithelial cell differentiation. Its interactions change, excluding flotillin 2 after differentiation, with phosphorylation not being essential.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Interactions
Background:
- Annexins are calcium- and phospholipid-binding proteins involved in cellular processes.
- Annexin A2 forms a heterotetramer with S100A10, participating in exocytosis, endocytosis, and cytoskeleton dynamics.
Purpose of the Study:
- To investigate annexin A2 cellular movements and identify its protein partners during epithelial cell differentiation.
- To understand how annexin A2 interactions change with epithelial cell differentiation.
Main Methods:
- Immunofluorescence microscopy
- Mass spectrometry (MS) for protein identification
- Western blot analysis
- S100A10 affinity chromatography
- Sucrose density gradient separation
Main Results:
- Identified E-cadherin, actin, and caveolin 1 as key annexin A2 binding partners.
- Annexin A2 associates with complexes of actin, caveolin 1, and flotillin 2 before differentiation.
- Post-differentiation, annexin A2 complexes include E-cadherin, actin, and caveolin 1, but exclude flotillin 2.
- Serine phosphorylation of annexin A2's N-terminal domain is not critical for epithelial cell differentiation.
Conclusions:
- Actin, caveolin 1, and E-cadherin are principal protein partners of annexin A2 in epithelial cells.
- Annexin A2 exhibits dynamic protein interactions during epithelial cell differentiation.
- The functional role of annexin A2 in epithelial differentiation is independent of N-terminal serine phosphorylation.
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