TY - JOUR
T1 - Cell type-specific requirements for heparan sulfate biosynthesis at the Drosophila neuromuscular junction
T2 - Effects on synapse function, membrane trafficking, and mitochondrial localization
AU - Ren, Yi
AU - Kirkpatrick, Catherine A.
AU - Rawson, Joel M.
AU - Sun, Mu
AU - Selleck, Scott B.
PY - 2009/7/1
Y1 - 2009/7/1
N2 - Heparan sulfate proteoglycans (HSPGs) are concentrated at neuromuscular synapses in many species, including Drosophila. We have established the physiological and patterning functions of HSPGs at the Drosophila neuromuscular junction by using mutations that block heparan sulfate synthesis or sulfation to compromise HSPG function. The mutant animals showed defects in synaptic physiology and morphology suggesting that HSPGs function both presynaptically and postsynaptically; these defects could be rescued by appropriate transgene expression. Of particular interest were selective disruptions of mitochondrial localization, abnormal distributions of Golgi and endoplasmic reticulum markers in the muscle, and a markedly increased level of stimulus-dependent endocytosis in the motoneuron. Our data support the emerging view that HSPG functions are not limited to the cell surface and matrix environments, but also affect a diverse set of cellular processes including membrane trafficking and organelle distributions.
AB - Heparan sulfate proteoglycans (HSPGs) are concentrated at neuromuscular synapses in many species, including Drosophila. We have established the physiological and patterning functions of HSPGs at the Drosophila neuromuscular junction by using mutations that block heparan sulfate synthesis or sulfation to compromise HSPG function. The mutant animals showed defects in synaptic physiology and morphology suggesting that HSPGs function both presynaptically and postsynaptically; these defects could be rescued by appropriate transgene expression. Of particular interest were selective disruptions of mitochondrial localization, abnormal distributions of Golgi and endoplasmic reticulum markers in the muscle, and a markedly increased level of stimulus-dependent endocytosis in the motoneuron. Our data support the emerging view that HSPG functions are not limited to the cell surface and matrix environments, but also affect a diverse set of cellular processes including membrane trafficking and organelle distributions.
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U2 - 10.1523/JNEUROSCI.5587-08.2009
DO - 10.1523/JNEUROSCI.5587-08.2009
M3 - Article
C2 - 19571145
AN - SCOPUS:67649965126
SN - 0270-6474
VL - 29
SP - 8539
EP - 8550
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 26
ER -