Psychiatry related information on mew

• Finally, overexpression of an alphaPS subunit throughout the wing leads to a dominant wing blister phenotype, and the critical period for this phenotype is the beginning of pupariation [1].

High impact information on mew

• The locus encodes two isoforms of a new alpha-integrin, a molecule that dynamically mediates cell adhesion and signal transduction [2].
• A particularly intriguing pattern of expression is found in the mature wing imaginal disc, where the PS1 integrin is expressed primarily on the presumptive dorsal wing epithelium, and the PS2 integrin is found almost exclusively on the ventral epithelium [3].
• We have also found that expression of PS1 in the visceral branch is regulated by the genes that direct tracheal cell migration, showing that integrin expression is part of the cell-fate program that they specify [4].
• PS3 antibodies bind to both dorsal and ventral disc cells and extract both PS1 and PS2 glycoprotein sets together with an additional component [5].
• Requirements for the cytoplasmic domain of the alphaPS1, alphaPS2 and betaPS integrin subunits during Drosophila development [6].

Biological context of mew

• A novel alpha integrin subunit associates with betaPS and functions in tissue morphogenesis and movement during Drosophila development [7].
• Vertebrate alpha PS1 and alpha PS2 family members are found on human chromosomes 2, 12, and 17 [8].

Anatomical context of mew

• The functions of PS1 and PS2 are specific in the two tissues, endoderm and mesoderm, since they cannot substitute for each other [9].
• The PS1 integrin is expressed in epidermal cells and can mediate adhesion of the epidermal HAJs to the basement membrane [10].
• PS1 expression is at the muscle ends and also in the long epidermal processes that connect the developing muscle fibers to their sites of attachment in the epidermis, while PS2 expression is restricted to the muscle ends [11].
• To this end we have analyzed muscle attachments and neuromuscular junctions ultrastructurally in single or double mutant Drosophila embryos lacking PS1 integrin (alphaPS1betaPS), PS2 integrin (alphaPS2betaPS), and/or their potential extracellular ligand laminin A [10].
• We have also examined the ability of alphaPS2 and alphaPS1 to maintain photoreceptor organization in the Drosophila retina [12].

Associations of mew with chemical compounds

• Thus, another integrin in addition to PS1 appears to function on the dorsal wing surface [13].
• The encoded alpha PS1 protein contains the cysteine pattern of the cleaved alpha integrins, three putative metal binding domains and shows the other characteristic features of alpha integrins [14].

Physical interactions of mew

• On mature wing discs, each class of position-specific (PS) antibody binds nonuniformly with respect to the dorso-ventral compartment boundary, with PS1 antibodies binding primarily to dorsal cells and PS2 antibodies, to ventral cells [15].

Other interactions of mew

• Nonequivalent requirements for PS1 and PS2 integrin at cell attachments in Drosophila: genetic analysis of the alpha PS1 integrin subunit [13].
• Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2 [16].

Analytical, diagnostic and therapeutic context of mew

• In this study we used time-lapse videomicroscopy to examine living embryos lacking both maternal and zygotic expression of the genes that encode the alpha PS1, alpha PS2, and beta PS integrin subunits [17].

References