ZFIN ID: ZDB-PUB-060306-3
Apical localization of ASIP/PAR-3:EGFP in zebrafish neuroepithelial cells involves the oligomerization domain CR1, the PDZ domains, and the C-terminal portion of the protein
von Trotha, J.W., Campos-Ortega, J.A., and Reugels, A.M.
Date: 2006
Source: Developmental dynamics : an official publication of the American Association of Anatomists 235(4): 967-977 (Journal)
Registered Authors: Campos-Ortega, Jose, Reugels, Alexander, von Trotha, Jakob
Keywords: zebrafish, neurulation, neuroepithelial polarity, asymmetric localization, spindle orientation, PAR-3, ASIP
MeSH Terms: Amino Acid Sequence; Animals; Caenorhabditis elegans Proteins/chemistry; Caenorhabditis elegans Proteins/genetics; Caenorhabditis elegans Proteins/metabolism (all 26) expand
PubMed: 16493684 Full text @ Dev. Dyn.
FIGURES   (current status)
ABSTRACT
Neurulation in zebrafish (Danio rerio) embryos is characterized by oriented cell divisions and the progressive establishment of cellular polarity. Mitoses in the neural plate and neural tube are planar, but in the neural keel/rod stage, the mitotic spindle rotates by 90 degrees, causing cell divisions to occur perpendicular to the plane of the neuroepithelium. The mechanisms and molecules that establish cellular polarity and cause the stereotypic orientation of the mitotic spindle during neurulation are largely unknown. In Caenorhabditis elegans and Drosophila, the PAR/aPKC complex has been shown to be involved in both establishment of cellular polarity and spindle orientation. Here, we show that the conserved N-terminal oligomerization domain (CR1) and the PDZ domains of ASIP/PAR-3:EGFP are involved in its localization to the apical membrane in zebrafish neuroepithelial cells. We further show that the C-terminal part of ASIP/PAR-3 contributes to proper localization and that the apical localization signals in ASIP/PAR-3 prevent the basolateral localization of a Numb:PAR-3 fusion protein. The parallel orientation of the mitotic spindle in the neural tube, however, is only weakly impaired upon overexpression of various ASIP/PAR-3:EGFP constructs.
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