File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: The drosophila ortholog of the endolysosomal membrane protein, endolyn, regulates cell proliferation

TitleThe drosophila ortholog of the endolysosomal membrane protein, endolyn, regulates cell proliferation
Authors
Issue Date2006
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503
Citation
Journal Of Cellular Biochemistry, 2006, v. 99 n. 5, p. 1380-1396 How to Cite?
AbstractEndolyn (CD164) is a sialomucin that regulates the proliferation, adhesion, and migration of human haematopoietic stem and progenitor cells. This molecule is predominately localized in endocytotic compartments, where it may contribute to endolysosomal biogenesis and trafficking. In order to more closely define the function of endolyn from an evolutionary view-point, we first analyzed endolyn orthologs in species ranging from insects, fish, and birds to mammals. The predicted molecular structures of the endolyn orthologs from these species are well conserved, particularly with respect to significant O-linked glycosylation of the extracellular domain, and the high degree of amino acid similarities within their transmembrane and cytoplasmic domains, with the latter possessing the lysosomal target signal, YXXφ. Focusing on Drosophila, our studies showed that the subcellular distribution of endolyn in non-polarized Drosophila S2 cells resembles that of its human counterpart in hematopoietic cells, with its predominant localization being within intracellular vesicles, while a small fraction occurs on the cell surface. Both Y → A and L → A mutations in the YHTL motif perturbed the normal subcellular distribution of Drosophila endolyn. Interestingly, embryonic and early larval development was often arrested in endolyn-deficient Drosophila mutants. This may partly be due to the role of endolyn in regulating cell proliferation, since knock-down of endolyn expression in S2 cells resulted in up to 50% inhibition of cell growth, with a proportion of cells undergoing apoptosis. Taken together, these results demonstrate that endolyn is an evolutionary conserved sialomucin fundamentally involved in cell proliferation in both the human and Drosophila melanogaster. © 2006 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/170094
ISSN
2015 Impact Factor: 3.446
2015 SCImago Journal Rankings: 1.520
References

 

DC FieldValueLanguage
dc.contributor.authorZhou, GQen_US
dc.contributor.authorZhang, Yen_US
dc.contributor.authorFerguson, DJPen_US
dc.contributor.authorChen, Sen_US
dc.contributor.authorRasmusonLestander, Åen_US
dc.contributor.authorCampbell, FCen_US
dc.contributor.authorWatt, SMen_US
dc.date.accessioned2012-10-30T06:05:16Z-
dc.date.available2012-10-30T06:05:16Z-
dc.date.issued2006en_US
dc.identifier.citationJournal Of Cellular Biochemistry, 2006, v. 99 n. 5, p. 1380-1396en_US
dc.identifier.issn0730-2312en_US
dc.identifier.urihttp://hdl.handle.net/10722/170094-
dc.description.abstractEndolyn (CD164) is a sialomucin that regulates the proliferation, adhesion, and migration of human haematopoietic stem and progenitor cells. This molecule is predominately localized in endocytotic compartments, where it may contribute to endolysosomal biogenesis and trafficking. In order to more closely define the function of endolyn from an evolutionary view-point, we first analyzed endolyn orthologs in species ranging from insects, fish, and birds to mammals. The predicted molecular structures of the endolyn orthologs from these species are well conserved, particularly with respect to significant O-linked glycosylation of the extracellular domain, and the high degree of amino acid similarities within their transmembrane and cytoplasmic domains, with the latter possessing the lysosomal target signal, YXXφ. Focusing on Drosophila, our studies showed that the subcellular distribution of endolyn in non-polarized Drosophila S2 cells resembles that of its human counterpart in hematopoietic cells, with its predominant localization being within intracellular vesicles, while a small fraction occurs on the cell surface. Both Y → A and L → A mutations in the YHTL motif perturbed the normal subcellular distribution of Drosophila endolyn. Interestingly, embryonic and early larval development was often arrested in endolyn-deficient Drosophila mutants. This may partly be due to the role of endolyn in regulating cell proliferation, since knock-down of endolyn expression in S2 cells resulted in up to 50% inhibition of cell growth, with a proportion of cells undergoing apoptosis. Taken together, these results demonstrate that endolyn is an evolutionary conserved sialomucin fundamentally involved in cell proliferation in both the human and Drosophila melanogaster. © 2006 Wiley-Liss, Inc.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503en_US
dc.relation.ispartofJournal of Cellular Biochemistryen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cd164 - Genetics - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCell Proliferationen_US
dc.subject.meshComputational Biologyen_US
dc.subject.meshDrosophila Proteins - Genetics - Metabolismen_US
dc.subject.meshDrosophila Melanogaster - Genetics - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMicroscopy, Immunoelectronen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshRna, Double-Stranded - Genetics - Metabolismen_US
dc.subject.meshRecombinant Fusion Proteins - Genetics - Metabolismen_US
dc.subject.meshSequence Alignmenten_US
dc.titleThe drosophila ortholog of the endolysosomal membrane protein, endolyn, regulates cell proliferationen_US
dc.typeArticleen_US
dc.identifier.emailZhou, GQ:wormoscz@gmail.comen_US
dc.identifier.authorityZhou, GQ=rp00527en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/jcb.20965en_US
dc.identifier.pmid16924678-
dc.identifier.scopuseid_2-s2.0-33751190312en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33751190312&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume99en_US
dc.identifier.issue5en_US
dc.identifier.spage1380en_US
dc.identifier.epage1396en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhou, GQ=23394245100en_US
dc.identifier.scopusauthoridZhang, Y=8918992000en_US
dc.identifier.scopusauthoridFerguson, DJP=7402014389en_US
dc.identifier.scopusauthoridChen, S=23003209800en_US
dc.identifier.scopusauthoridRasmusonLestander, Å=6603628666en_US
dc.identifier.scopusauthoridCampbell, FC=35494431000en_US
dc.identifier.scopusauthoridWatt, SM=7102659490en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats