title: The adaptor protein X11Lalpha/Dmint1 interacts with the PDZ-binding domain of the cell recognition protein Rst in Drosophila.
abstract: 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.
authors.affiliation: Institut für Biologie III, Albert-Ludwigs Universität, D-79104 Freiburg im Breisgau, Germany.
authors.forename: Smitha
authors.initials: S
authors.lastname: Vishnu
authors.forename: Alexander
authors.initials: A
authors.lastname: Hertenstein
authors.forename: Jörg
authors.initials: J
authors.lastname: Betschinger
authors.forename: Jürgen A
authors.initials: JA
authors.lastname: Knoblich
authors.forename: H
authors.initials: H
authors.lastname: Gert de Couet
authors.forename: Karl-Friedrich
authors.initials: KF
authors.lastname: Fischbach
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules; D015816:Cell Adhesion Molecules, Neuronal / Q000235:genetics / Q000378:metabolism*; D004330:Drosophila / Q000196:embryology / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D019143:Evolution, Molecular; D005123:Eye / Q000196:embryology / Q000378:metabolism; D005136:Eye Proteins / Q000235:genetics / Q000378:metabolism*; D018613:Microscopy, Confocal; D008957:Models, Genetic; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D020033:Protein Isoforms / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D011679:Pupa / Q000254:growth & development; D020798:Two-Hybrid System Techniques
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D015815:Cell Adhesion Molecules; D015816:Cell Adhesion Molecules, Neuronal; D029721:Drosophila Proteins; D005136:Eye Proteins; D009687:Nuclear Proteins; D020033:Protein Isoforms; C498473:X11L protein, Drosophila; C085209:rst protein, Drosophila