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Calcyon Regulates Axonal Transport of PI4K11a Vesicles in Cultured Rat Sensory Neurons
Author(s) -
Roth Zak,
Shi Liang,
Smith Deanna
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.727.3
Subject(s) - dynein , axon , microbiology and biotechnology , vesicular transport protein , axoplasmic transport , biology , vesicle , motor protein , endosome , microtubule , axoplasm , dynactin , neurodegeneration , neurite , neuroscience , biochemistry , intracellular , in vitro , membrane , medicine , disease , pathology
Cytoplasmic dynein is a motor protein representing an essential component in directed microtubule trafficking of membrane bound vesicles. Dynein motors are primarily responsible for retrograde, or minus‐end directed axon transport. Recently, we have shown that Calcyon (Caly, NSG3), a type 2 transmembrane protein important for the targeting of Clathrin Adaptor Protein‐3 (AP3) cargos, interacts with dynein (Muthusamy et al, in preparation). In order to explore Caly's viability as an efficient regulator of dynein activity, we have used time‐lapse microscopy and kymographs to analyze axonal trafficking of PI4K11a organelles in cultured adult rat sensory neurons. PI4K11a is a known Calcyon‐interacting protein involved in endosomal trafficking. The motility of organelles enriched in PI4K11a was shown to be altered by changes in Calcyon expression. In addition, previous studies indicate that the loss of PI4K11a in mice results in an adult onset neurodegeneration phenotype (Simons et al, PNAS, 2009). Based on our studies, we hypothesize that the Caly/PI4K11a interaction is an important regulator of dynein‐dependent axon transport, and any significant disruption of this interaction has the potential to cause axon degeneration.