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Molecular and Cellular Biology, November 2006, p. 7991-7998, Vol. 26, No. 21
0270-7306/06/$08.00+0     doi:10.1128/MCB.00904-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

ZP2 and ZP3 Traffic Independently within Oocytes prior to Assembly into the Extracellular Zona Pellucida

Tanya Hoodbhoy,1 Manuel Avilés,2 Boris Baibakov,1 Olga Epifano,1 María Jiménez-Movilla,2 Lyn Gauthier,1 and Jurrien Dean1*

Laboratory of Cellular and Developmental Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892,1 Department of Cell Biology, Medical School, Campus de Espinardo, University of Murcia, E-30071 Murcia, Spain2

Received 20 May 2006/ Accepted 24 July 2006

The extracellular zona pellucida surrounds mammalian eggs and mediates taxon-specific sperm-egg recognition at fertilization. In mice, the zona pellucida is composed of three glycoproteins, but the presence of ZP2 and ZP3 is sufficient to form a biologically functional structure. Each zona pellucida glycoprotein is synthesized in growing oocytes and traffics through the endomembrane system to the cell surface, where it is released from a transmembrane domain and assembled into the insoluble zona pellucida matrix. ZP2 and ZP3 colocalize in the endoplasmic reticulum and in 1- to 5-µm post-Golgi structures comprising multivesicular aggregates (MVA), but a coimmunoprecipitation assay does not detect physical interactions. In addition, ZP2 traffics normally in growing oocytes in the absence of ZP3 or if ZP3 has been mutated to prevent incorporation into the zona pellucida matrix, complementing earlier studies indicating the independence of ZP3 secretion in Zp2 null mice. N glycosylation has been implicated in correct protein folding and intracellular trafficking of secreted proteins. Although ZP3 contain five N-glycans, enhanced green fluorescent protein-tagged ZP3 lacking N glycosylation sites is present in MVA and is incorporated into the zona pellucida matrix of transgenic mice. Thus, ZP2 secretion is seemingly unaffected by ZP3 lacking N-glycans. Taken together, these observations indicate that ZP2 and ZP3 traffic independently through the oocyte prior to assembly into the zona pellucida.

* Corresponding author. Mailing address: Laboratory of Cellular and Developmental Biology, NIDDK, Building 50, Room 3134, National Institutes of Health, Bethesda, MD 20892-8028. Phone: (301) 496-2738. Fax: (301) 496-5239. E-mail: jurrien{at}helix.nih.gov.

Molecular and Cellular Biology, November 2006, p. 7991-7998, Vol. 26, No. 21
0270-7306/06/$08.00+0     doi:10.1128/MCB.00904-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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