ALG-2 oscillates in subcellular localization, unitemporally with calcium oscillations.
Research output: Contribution to journal › Journal article › Research › peer-review
A variety of stimuli can trigger intracellular calcium oscillations. Relatively little is known about the molecular mechanisms decoding these events. We show that ALG-2, a Ca2+-binding protein originally isolated as a protein associated with apoptosis, is directly linked to Ca2+ signalling. We discovered that the subcellular distribution of a tagged version of ALG-2 could be directed by physiological external stimuli (including ATP, EGF, prostaglandin, histamine), which provoke intracellular Ca2+ oscillations. Cellular stimulation led to a redistribution of ALG-2 from the cytosol to a punctate localization in an oscillatory fashion unitemporally with Ca2+ oscillations, whereas a Ca2+-binding deficient mutant of ALG-2 did not redistribute. Using tagged ALG-2 as bait we identified its novel target protein Sec31A and based on the partial colocalization of endogenous ALG-2 and Sec31A we propose that ALG-2 temporarily binds to the COPII vesicles providing a link between Ca2+ signalling and ER to Golgi trafficking.
Udgivelsesdato: 2007-Feb-23
Udgivelsesdato: 2007-Feb-23
Original language | English |
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Journal | Biochemical and Biophysical Research Communications |
Volume | 353 |
Issue number | 4 |
Pages (from-to) | 1063-7 |
Number of pages | 4 |
ISSN | 0006-291X |
DOIs | |
Publication status | Published - 2007 |
Bibliographical note
Keywords: Adenosine Triphosphate; Apoptosis Regulatory Proteins; Calcium; Calcium Signaling; Calcium-Binding Proteins; Carrier Proteins; Cell Line, Tumor; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Green Fluorescent Proteins; Hela Cells; Histamine; Humans; Immunohistochemistry; Immunoprecipitation; Microscopy, Confocal; Mutation; Protein Binding; Protein Transport; Recombinant Fusion Proteins; Time Factors; Transfection; Vesicular Transport Proteins
ID: 3137605