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Vol. 11, Issue 8, 2757-2773, August 2000
Columbia University, Department of Microbiology, New York, New York
10032
mid1 is required for the proper placement of the
contractile actin ring for cytokinesis at a medial site overlying the
nucleus. Here we find that mid1 protein (mid1p) shuttles between the
nucleus and a cortical medial broad band during interphase and early
mitosis. The position of this broad band, which overlies the nucleus,
is linked to nuclear position even in cells with displaced or multiple nuclei. We identified and created mutations in an NLS and in two crm1-dependent NES sequences in mid1p. NES mutations caused mid1p accumulation in the nucleus and loss of function. An NLS mutations greatly reduced nuclear localization but did not perturb cytoplasmic localization or function. mid1p localization to the medial broad band
was also not dependent on mid1p PH domain or microtubule and actin
cytoskeletons. Overexpression of mid1p produced ectopic cell growth at
this band during interphase and abnormal karmellae-like nuclear
membrane structures. In plo1-1, mid1p formed a medial broad band but did not incorporate into a tight ring, suggesting that
polo kinase plo1p is required for activation of mid1p function. Thus,
the mid1p broad band defines a compartment at the medial cell surface,
whose localization is linked to the position of the nucleus, and whose
function may be to position the plane of cell division.
Corresponding author. E-mail address:
fc99{at}columbia.edu.
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