NDLI: The N terminus of the Drosophila Numb protein directs membrane association and actin-dependent asymmetric localization.

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The N terminus of the Drosophila Numb protein directs membrane association and actin-dependent asymmetric localization.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Knoblich, J. A. Jan, Y. N. Jan, L. Y.
Description	Author Affiliation: Knoblich JA ( Department of Physiology, Howard Hughes Medical Institute, University of California, San Francisco 94143-0724, USA.);
Abstract	Drosophila Numb is a membrane associated protein of 557 amino acids (aa) that localizes asymmetrically into a cortical crescent in mitotic neural precursor cells and segregates into one of the daughter cells, where it is required for correct cell fate specification. We demonstrate here that asymmetric localization but not membrane localization of Numb in Drosophila embryos is inhibited by latrunculin A, an inhibitor of actin assembly. We also show that deletion of either the first 41 aa or aa 41-118 of Numb eliminates both localization to the cell membrane and asymmetric localization during mitosis, whereas C-terminal deletions or deletions of central portions of Numb do not affect its subcellular localization. Fusion of the first 76 or the first 119 aa of Numb to beta-galactosidase results in a fusion protein that localizes to the cell membrane, but fails to localize asymmetrically during mitosis. In contrast, a fusion protein containing the first 227 aa of Numb and beta-galactosidase localizes asymmetrically during mitosis and segregates into the same daughter cell as the endogenous Numb protein, demonstrating that the first 227 aa of the Numb protein are sufficient for asymmetric localization.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Drosophila Metabolism Juvenile Hormones Animals Bicyclo Compounds, Heterocyclic Pharmacology Drosophila Proteins Chemistry Genetics Myristic Acid Thiazoles Thiazolidines Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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