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The cellular and developmental expression of hrs‐2 in rat
Author(s) -
Tsujimoto S.,
PeltoHuikko M.,
Aitola M.,
Meister B.,
VikMo E. O.,
Davanger S.,
Scheller R. H.,
Bean A. J.
Publication year - 1999
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1046/j.1460-9568.1999.00716.x
Subject(s) - microbiology and biotechnology , biology , cytoplasm , messenger rna , vesicle , secretion , transport protein , membrane , biochemistry , gene
Abstract The molecular events underlying vesicular trafficking probably involve the formation and dissolution of protein complexes between integral components of the vesicle and its target membrane. SNAP‐25 is associated with the plasma membrane and is a component of a core protein complex thought to be essential for neurotransmitter release. We have previously characterized a protein, hrs‐2, that interacts with SNAP‐25 and inhibits secretion from permeabilized PC12 cells. The cellular localization and developmental expression patterns of a number of proteins involved in the secretion machinery have been documented. To understand more about the possible cellular role of hrs‐2, we have examined hrs‐2 distribution, developmental expression and subcellular localization in rat tissues and cell lines. We show herein that the distribution of hrs‐2 in brain and periphery parallels that of SNAP‐23/25, and that recombinant hrs‐2 binds to both SNAP‐23 and SNAP‐25. Hrs‐2 mRNA and protein are found almost ubiquitously in neurons in the brain. Hrs‐2 mRNA is expressed in the neural tube at E10 and thereafter mRNA and protein levels remain relatively constant in the whole brain through adulthood. In cultured PC12 cells, endogenous hrs‐2 is expressed in the cytoplasm and on the limiting membranes of multivesicular bodies. Overexpression of hrs‐2 in mammalian cells results in the appearance of large intracellular compartments that are labelled with hrs‐2 antibodies. The wide distribution, the interaction with SNAP‐23 and the localization on multivesicular body membranes suggest a general role for hrs‐2 in cellular machinery.