Related Experiment Video
Updated: Aug 15, 2026

In Vivo Imaging of Muscle-tendon Morphogenesis in Drosophila Pupae
Published on: February 6, 2018
A novel alpha integrin subunit associates with betaPS and functions in tissue morphogenesis and movement during
Abstract:
We have identified a novel alpha integrin subunit in Drosophila, that associates with betaPS integrin. We report the temporal expression of the gene encoding this integrin subunit, which we have called alphaPS3, throughout development and the localization of its expression during embryogenesis. AlphaPS3 RNA was localized to tissues undergoing invagination, tissue movement and morphogenesis such as salivary gland, trachea, midgut, dorsal vessel, midline of the ventral nerve cord, amnioserosa and the amnioproctodeal invagination. AlphaPS3 DNA localized to the chromosomal vicinity of scab (scb), previously identified by a failure of dorsal closure. Embryos homozygous for the 119 allele of scb had no detectable alphaPS3 RNA and the 1035 allele of scb contains a P element inserted just 5' of the coding region for the shorter of the gene's two transcripts. Furthermore, mutations in the scb locus exhibit additional defects corresponding to sites of alphaPS3 transcription, including abnormal salivary glands, mislocalization of the pericardial cells and interrupted trachea. Removal of both maternal and zygotic betaPS produced similar defects, indicating that these two integrin subunits associate in vivo and function in the movement and morphogenesis of tissues during development in Drosophila. Phenotypic similarities suggest that laminin A is a potential ligand for this integrin, at least in some tissues.
More Related Videos
07:15A Cell-based Assay to Investigate Non-muscle Myosin II Contractility via the Folded-gastrulation Signaling Pathway in Drosophila S2R+ Cells
Published on: August 19, 2018
12:35Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
Published on: April 14, 2023
Related Concept Videos
Fibronectins Connect Cells with ECM
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Laminins are the Adhesive Proteins of Basal Lamina
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
Integrins
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Activation of Integrins
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Intracellular Signaling Affects Focal Adhesions
Some...
Anchoring Junctions