Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1998-1-8
pubmed:abstractText
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-1649700, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-1673362, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-1720353, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-1733500, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-2121610, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-2515889, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-2516798, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-2517255, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-2752427, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-2776221, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-2991884, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-6681676, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-6684994, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-7514424, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-7534213, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-7566172, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-7566173, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-7588053, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8223268, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8313469, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8582263, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8625408, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8625409, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8626022, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8684486, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8755475, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8755476, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8779714, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-8876239, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-9128251, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-9219698, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371790-9288973
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13005-10
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The N terminus of the Drosophila Numb protein directs membrane association and actin-dependent asymmetric localization.
pubmed:affiliation
Department of Physiology, Howard Hughes Medical Institute, University of California, San Francisco 94143-0724, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't