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A more recent version of this article appeared on September 1, 2003
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Submitted on October 8, 2002
Revised on April 4, 2003
Accepted on April 23, 2003
1 Department of Biological Sciences, Columbia University, New York, NY 10027, U.S.A.
* Corresponding author. E-mail address: ms2001{at}columbia.edu.
Axonal transport of membranous organelles such as mitochondria is
essential for neuron viability and function. How signaling mechanisms
regulate or influence mitochondrial distribution and transport is still
largely unknown. We observed an increase in the distal distribution of
mitochondria in neurons upon the expression of pleckstrin homology (PH)
domains of phospholipase C
1 (PLC-PH) and spectrin (spectrin-PH).
Quantitative analysis of mitochondrial transport showed that specific
binding of PH domains to phosphatidylinositol (4,5)
bisphosphate (PtdIns(4,5)P2) but not 3' phosphorylated
phosphatidylinositol species enhanced plus-end directed
transport of mitochondria 2-3 fold and at the same time decreased
minus-end directed transport of mitochondria along axonal microtubules
(MTs) without altering the overall level of motility. Further, the
velocity and duration of mitochondrial transport plus the association
of molecular motors with mitochondria remained unchanged by the
expression of PH domains. Thus, PtdIns(4,5)P2-specific PH domains
caused an increase in distal mitochondria by disturbing the balance of
plus-end and minus-end directed transport rather than directly
affecting the molecular machinery involved. Taken together our data
reveals that level and directionality of transport are separable and
that PtdIns(4,5)P2 has a novel role in regulation of the directionality
of axonal transport of mitochondria.
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