Full PapersPS2 Integrin Requirements in Drosophila Embryo and Wing Morphogenesis
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Integrins in Development
2012, Integrins: Molecular and Biological Responses to the Extracellular MatrixCell adhesion in Drosophila: versatility of cadherin and integrin complexes during development
2012, Current Opinion in Cell BiologyCitation Excerpt :There does not appear to be a similar ‘core’ of intracellular proteins that can be co-purified with integrins; this may be due to the technical difficulties of purifying integrins bound to the insoluble extracellular matrix, or it may reflect a lower affinity in the interactions, with chemical cross-linking being required to co-purify any of the integrin-associated proteins from cultured cells [78]. A large number of proteins fulfill criterion 2 ([Table 3]). Comparing muscle attachment sites (the major site of integrin adhesion in the embryo) to the focal adhesion structures that form on the basal surface of the follicular epithelium revealed that 7 of the 9 components examined were present in both systems [21].
Born to run: Creating the muscle fiber
2010, Current Opinion in Cell BiologyCitation Excerpt :Genetic disruption of the muscle αPS2βPS integrin does not interfere with construction, elongation, and attachment of muscle fibers. However, once the muscles of such mutant embryos begin to contract, they disconnect from their attachment sites and retract into ball-shaped structures [60–63]. This classic ‘myospheroid’ phenotype now serves as a diagnostic tool for identification of additional elements contributing to formation and consolidation of myotendinous junctions.
An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand
2010, Journal of Biological ChemistryCitation Excerpt :We next investigated whether a genetic interaction exists between pgant3 mutants and an αPS2 integrin mutant (if3). if3 mutants are hypomorphic and show a low level of wing blistering in a wild type background (9). Flies hemizygous for if3 in combination with the chromosome 2 used for mutagenesis (if3/Y; +/+) displayed 17% wing blistering (Table 2).
Integrins during evolution: Evolutionary trees and model organisms
2009, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :We have also seen that large amino-terminal regions of both the α and β subunits that respectively code for the β propeller and the βI domain in the integrins are found in protein sequences from bacteria (see below). The general function of the integrins – a role in cell adhesion and communication – appears to have been established early as well and has been well characterized in several invertebrates (for a review, see [15]) such as in C. elegans where two α subunits (Ina-1, Pat-2) and one β subunit (Pat-3) [16–18] are found and five α and two β subunits in Drosophila[19–25]. In vertebrates, the integrin subunits have diversified to accommodate additional functions with roles that likely relate to the large changes that occurred during chordate evolution in the transition to cartilaginous and bony internal structures, a dual innate and adaptive immune system and the high-pressure circulatory system that characterize the vertebrate lineage.