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J. Cell Biol.,
Volume 144, Number 6, March 22, 1999 1323-1336
Department of Molecular Biology and Microbiology, Case Western Reserve University, School of Medicine, Cleveland,
Ohio 44106-4960
Cell adhesion is critical to the establishment
of proper connections in the nervous system. Some receptor-type protein tyrosine phosphatases (RPTPs)
have adhesion molecule-like extracellular segments
with intracellular tyrosine phosphatase domains that may transduce signals in response to adhesion. PTPµ is
a RPTP that mediates cell aggregation and is expressed
at high levels in the nervous system. In this study, we
demonstrate that PTPµ promotes neurite outgrowth of
retinal ganglion cells when used as a culture substrate.
In addition, PTPµ was found in a complex with N-cadherin in retinal cells. To determine the physiological significance of the association between PTPµ and N-cadherin, the expression level and enzymatic activity of
PTPµ were perturbed in retinal explant cultures.
Downregulation of PTPµ expression through antisense
techniques resulted in a significant decrease in neurite
outgrowth on an N-cadherin substrate, whereas there was no effect on laminin or L1-dependent neurite outgrowth. The overexpression of a catalytically inactive
form of PTPµ significantly decreased neurite outgrowth on N-cadherin. These data indicate that PTPµ
specifically regulates signals required for neurites to extend on an N-cadherin substrate, implicating reversible
tyrosine phosphorylation in the control of N-cadherin
function. Together, these results suggest that PTPµ
plays a dual role in the regulation of neurite outgrowth.
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