Open Close
Vishnu, S., Hertenstein, A., Betschinger, J., Knoblich, J.A., de Couet, G.H., Fischbach, K.F. (2006). The adaptor protein X11Lalpha/Dmint1 interacts with the PDZ-binding domain of the cell recognition protein Rst in Drosophila.  Dev. Biol. 289(2): 296--307.
FlyBase ID
Publication Type
Research paper

The Drosophila cell adhesion molecule Rst plays key roles during the development of the embryonic musculature, spacing of ommatidia in the compound eye and of sensory organs on the antenna, as well as in the neuronal wiring of the optic lobe. In rst(CT) mutants lacking the cytoplasmic domain of the Rst protein, cell sorting and apoptosis in the eye are affected, suggesting a requirement of this domain for Rst function. To identify potential interacting proteins, yeast two-hybrid screens were performed using the cytoplasmic domains of Rst and its paralogue Kirre as baits. Among several putative interactors, two paralogous Drosophila PDZ motif proteins related to X11/Mint were identified. X11/Mint family members in C. elegans (LIN-10) and vertebrates are believed to function as adaptor proteins and to regulate the assembly of multi-subunit complexes at the synapse, thereby linking the vesicle cycle to cell adhesion. Using genetic, cell biological, and biochemical approaches, we show that the interaction of Rst with X11Lalpha is of biological significance. The proteins interact, for example, in the context of cell sorting in the pupal retina.

PubMed ID
PubMed Central ID
Associated Information
Associated Files
Other Information
Secondary IDs
    Language of Publication
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Dev. Biol.
    Developmental Biology
    Publication Year
    Data From Reference
    Alleles (9)
    Genes (6)
    Physical Interactions (5)
    Natural transposons (1)
    Insertions (1)
    Experimental Tools (3)
    Transgenic Constructs (6)