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J Biol Chem, Vol. 274, Issue 6, 3257-3260, February 5, 1999
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From the Clathrin-mediated endocytosis was shown to be
arrested in mitosis due to a block in the invagination of
clathrin-coated pits. A Xenopus mitotic phosphoprotein,
MP90, is very similar to an abundant mammalian nerve terminal protein,
epsin, which binds the Eps15 homology (EH) domain of Eps15 and the
Howard Hughes Medical Institute and
Department of Cell Biology, Yale University School of Medicine, New
Haven Connecticut 06510, the § Department of Experimental
Oncology, European Institute of Oncology, Milan 20141, Italy, and the
¶ Istituto di Microbiologia, Universitá di Bari,
Bari 70124, Italy
-adaptin subunit of the clathrin adaptor AP-2. We show here that
both rat epsin and Eps15 are mitotic phosphoproteins and that their
mitotic phosphorylation inhibits binding to the appendage domain of
-adaptin. Both epsin and Eps15, like other cytosolic components of
the synaptic vesicle endocytic machinery, undergo constitutive
phosphorylation and depolarization-dependent dephosphorylation
in nerve terminals. Furthermore, their binding to AP-2 in brain
extracts is enhanced by dephosphorylation. Epsin together with Eps15
was proposed to assist the clathrin coat in its dynamic
rearrangements during the invagination/fission reactions.
Their mitotic phosphorylation may be one of the mechanisms by which the
invagination of clathrin-coated pits is blocked in mitosis and their
stimulation-dependent dephosphorylation at synapses may
contribute to the compensatory burst of endocytosis after a secretory stimulus.
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