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Association of Caldendrin splice isoforms with secretory vesicles in neurohypophyseal axons and the pituitary
Author(s) -
Landwehr Marco,
Redecker Peter,
Dieterich Daniela C.,
Richter Karin,
Böckers Tobias M.,
Gundelfinger Eckart D.,
Kreutz Michael R.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00713-0
Subject(s) - gene isoform , splice , postsynaptic potential , microbiology and biotechnology , alternative splicing , synaptic vesicle , secretory vesicle , biology , vesicle , chemistry , neuroscience , gene , biochemistry , receptor , membrane
Caldendrin is a neuronal calcium‐binding protein, which is highly enriched in the postsynaptic density fraction and exhibits a prominent somato‐dendritic distribution in brain. Two additional splice variants derive from the caldendrin gene, which have unrelated N‐termini and were previously only detected in the retina. We now show that these isoforms are present in neurohypophyseal axons and on secretory granules of endocrine cells. In light of the described interaction of the Caldendrin C‐terminus with Q‐type Ca v 2.1 calcium channels these data suggest that this interaction takes place in neurohypophyseal axons and pituitary cells indicating functions of the short splice variants in triggering Ca 2+ transients to a vesicular target interaction.