βPS, βPS integrin, β-integrin, βPS-integrin, βPS
transmembrane protein - integrin-beta subunit of PS1 & PS2 - integrins are used to attach mesoderm to ectoderm and are required for the proper assembly of the extracellular matrix and for muscle attachment - functions in signaling between presynaptic and postsynaptic compartments of the neuromuscular junction
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Annotated transcripts do not represent all possible combinations of alternative exons and/or alternative promoters.
Annotated transcripts do not represent all supported alternative splices within 5' UTR.
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.50
846 (aa); 90 (kD predicted)
Heterodimer of an alpha and a beta subunit. Beta-PS associates with either alpha-PS1, alpha-PS2, alpha-PS3, alpha-PS4 or alpha-PS5.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\mys using the Feature Mapper tool.
Immunostaining withantibodies against βPS integrin mys shows that it strongly accumulates at the basement membrane throughout the midgut, and also specifically at all surface membranes of ISCs and EBs, but weakly in ECs.
mys released from border cells during migration was visible as discrete puncta behind the border cells in the anterior part of the wild-type egg chambers.
mys staining is observed along lateral, apical, and basal follicle cell membranes through stage 10A. Apical staining peaks in stage 9 and 10A columnal follicle cells overlying the oocyte while downregulating in the most posterior follicle cells. Expression is also seen in border cells at intercellular junctions. After stage 10A, the remaining follicle cell populations begin down-regulating apically localized mys while maintaining lateral and basal localization during dorsal appendage morphogenesis.
mys protein is localized to both germline and somatic cells in the germarium, but is restricted to follicle cells later in oogenesis. It is concentrated to the basolateral side of cells, but also has some apical localization.
mys is found to localize at the interface between wing disc cells and tracheal branches in the embryo.
The mys protein is enriched at the muscle-tendon junction in third instar larvae and is found in both the tendon cell and the muscle cell. The expression pattern partially overlaps that of the shot protein.
Protein is detected in the muscle attachment sites underneath the hypoderm in stage 15-16 embryos.
the greatest concentration of mys protein is found at somatic muscle attachment sites. Staining is also observed in the pharynx, midgut, and hindgut.
Only a faint residual band of protein is seen on immunoblots of mysXB87 mutant embryos. This is thought to be a remnant from the maternal supply. No staining is seen at muscle attachment sites.
GBrowse - Visual display of RNA-Seq signalsView Dmel\mys in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
"l(1)968" may correspond to "mys".
Originally isolated (Rodrigues and Siddiqi, 1978) in the same 'then-unnamed' manner as olfA, olfB and olfD (the latter = sbl).
Mutations at residue 409 increase ligand binding.
mys is required for maintenance of tracheal terminal branches and luminal organization.
Strong mys alleles fail to complement antimorphic mys alleles at all temperatures. Weak mys alleles are able to complement antimorphic mys alleles at low temperatures. The lethality of mys hemizygotes is increased when mutants are also mew or if heterozygotes.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
RNAi screen using dsRNA made from templates generated with primers directed against this gene causes a phenotype when assayed in S2R+ cells: cells become round and detached. Kc167 cells are unaffected.
mys at the postembryonic neuromuscular junction is a critical determinant of morphological growth and synapse specificity.
Identification: Directed mosaic screen for lethally mutable loci having an effect in the follicular epithelium.
The functional significance of the cytoplasmic domains of the if, mew and mys subunits of the Position Specific (PS) integrin family are studied by analysing the relationship between the cytoplasmic domain structure and function in the context of a developing organism. Although many events require the mys cytoplasmic domain, this portion of the molecule is not required for at least two processes requiring PS integrins: formation of midgut constrictions and maintaining germband integrity. Mutation of residues in the cytoplasmic tail function suggest that interaction of the PS integrins with cytoplasmic ligands is developmentally modulated during embryogenesis.
if and mys can be localised by an intracellular mechanism within the muscles. Direct localisation of the transmembrane protein to sites of integrin function occurs in cells that lack endogenous mys and if or cells that lack extracellular signals from the tendon cells.
The retinal phenotypes of integrin mutants trace their origin to the structural failure of the cone cell plate and the focal adhesions of the pigment cells.
mys transmembrane and cytoplasmic domain contains sufficient information to target the integrins to the muscle attachment sites.
hh, wg and mys are required for epithelial morphogenesis during proventriculus organ development. The morphogenetic process is suppressed by dpp. These results identify a novel cell signalling centre in the foregut that operates through a distinct genetic circuitry in the midgut to direct the formation of a multiply folded organ from a simple epithelial tube.
Phenotypic analysis of mew, if and mys embryos suggests multiple roles for PS integrins in the adhesion of cells and in the formation, organization and migration of embryonic tissues. Although the proteins are often expressed in adjacent embryonic tissues, this distribution does not necessarily reflect equivalent requirements. The complete loss of both α subunits, encoded by mew and if, does not produce all the phenotypes observed in embryos lacking the mys encoded β subunit.
Mutant alleles can affect axonal pathfinding and glial cell migration in the developing optic lobe.
Comparison of the null phenotypes of mys (encoding the ΒPS integrin subunit) and if rules out a model where PS integrin function occurs solely by the direct interaction of the two PS integrins, αPS1ΒPS and αPS2ΒPS.
Analysis of a series of mys mutants reveals that the efficiency with which the mutant proteins function in different morphogenetic processes varies greatly, suggesting that the cytoplasmic interactions involving PS integrins are developmentally modulated.
Muscle phenotype of mutants studied using polarised light microscopy and antibody staining to detect Mhc-lacZ reporter gene expression in muscles.
The distribution of LanA and mys products in wing development suggests that laminin is not a ligand for integrin in this context.
The PS integrins are required throughout pupation for wing development, but only during late pupation for eye development. They are not required for the differentiation of ommatidial cells, only for their organization. They maintain interactions between the wing epithelia during the two phases of pupal wing expansion and in the attachment of a fully formed fenestrated membrane to the basement membrane of the retina. A requirement for the alternative splicing of the mys transcript during embryogenesis has been demonstrated.
PS2 integrin is expressed on the surface of cells and can mediate cell spreading on an undefined component of fetal calf serum, on the purified vertebrate matrix molecules vitronectin and fibronectin, and on RGD peptide. Spreading can be inhibited by soluble RGD peptide and is dependent on divalent cations.
The requirement for integrins during development has been studied using animals mosaic for mys mutations. Expression of mys is required in many parts of the developing fly, with an especially large requirement in ventrally derived tissues.
mys function is required for muscle formation and proper CNS development. Mutants in mys specifically affect the tergal depressor of the trocanter.
Mutagenesis of mysolfC-x17 led to some strains with 'stronger' acetate-based olfactory deficit than the starting mutant. In one of these called "olfCx17-1a", responses to iso-amyl acetate worse than in mysolfC-x17 and the new strain also shows reduction in responses to benzaldehyde; both of these abnormalities covered by Dp(1;2)sn+72d and uncovered by Df(1)ct-J4, apparently placing this novel genetic defect in 7A2-C1, a region separate from olfC.
Structural gene for the β subunit of position-specific integrins 1 and 2, PS1 and PS2. Twenty-hour embryos (25oC) show middorsal herniation of brain and midgut, or both; abnormal somatic, visceral and pharyngeal muscles; and incomplete morphogenesis of yolk-filled midgut. Development of embryo normal up to 13 hr, even in embryos produced from homozygous germ-line clones (Wieschaus and Noell, 1986). Between 13 and 14.5 hr the first muscular contractions occur, while basement membrane is incomplete. This results in dorsal rupture of hypoderm and retraction of myogenic elements of somatic and pharyngeal muscles into spheroidal masses. Continuation of myogenesis produces spheroidal muscles with a cortex of disoriented fibrillae surrounded by a medulla of nucleated sarcoplasm. Homozygous clones of mys11 on either surface of the wing lead to separation of the two surfaces of the membrane and the formation of blisters in the vicinity of the clone (Brower and Jaffe, 1989). Western blots with antibodies specific to the β subunit of Drosophila PS integrins detects no β integrin in mys10, mys11 and Df(1)C128; in addition, PS1α is not cleaved properly in these genotypes, nor do α chains become localized in mutant embryos. PSβ expression in wild type is diffuse in early embryos, becoming localized between the mesodermal and ectodermal layers at the extended-germ-band stage; also seen at interfaces between epidermal cells and deep in the intersegmental grooves where intersegmental muscles attach. In late embryos antibody staining is seen at basal surface of entire gut epithelium and is also concentrated at muscle attachment sites. Information related to olfC alleles: Adults show poor responses to acetates and acetone and have diminished responses to some alcohols, in tests involving Y-tube olfactometer (Rodrigues, 1980). Odor-induced jump assays on mysolfC-x3 and mysolfC-x17 adults (Ayyub et al., 1990) gave results paralleling those using olfactometer (whereby these mutants are in one of two different 'acetate defective' categories; see alleles). Larvae respond abnormally to acetetes and normally to aldehydes (Rodrigues, 1980). Electroantennograms (EAGs) recorded from adults show olfC to exhibit diminished responses of olfactory receptors to acetates (Venard and Pichon, 1984) and to 2-butanone as well (Venard et al., 1989). Similar physiological (Siddiqi, 1984) and also behavioral (Rodrigues, 1980), experiments involving pairs of odorants, e.g. ethyl and iso-amyl acetate, suggested more than one independent 'channel' for the reception of these substances. In SEM observations (Venard et al., 1989) mutant antenna seems to have normal number and distribution of the three kinds of sensilla on the anterior face of the funiculus (from where EAGs recorded). Electrophoresis of triton extracts of antennae generates an extra band of esterase activity in olfC, which is found in neither wild-type nor in mutant thoraces and abdomens (Venard et al., 1989). olfC males fail to have their courtship of wild-type males inhibited by high concentrations of volatile compounds (unlike normal males, which are inhibited). Mutant males court other males with abnormally high vigor yet court females with subnormal intensity (Tompkins et al., 1981). Further studies showed that the mutant courts immature males vigorously (as do wild-type males) and this wanes as the courtee ages, but not to the same extent as in normal pairings; the inappropriately high levels of olfC courtships directed at maturing males includes all sex behaviors except attempted copulation (Curcillo and Tompkins, 1987). An inability of mutant males to discriminate between recently mated and virgin females was reported by Mane et al. (1983), who also showed that olfC males can detect, 6 hours post insemination, a difference between females mated to Est-60 males vs. males carrying a non-null allele of this gene (the latter kind of mated females were said to be relatively inhibitory to male courtship); these experiments suggested that the enzyme encoded by Est-6 turns a 'pre-anti-aphrodisiac' compound, cis-vaccenyl acetate, which is transferred from males to females during copulation into a further, or the actual aphrodisiac, cis-vaccenyl alcohol; some elements of such results and inferences (Mane et al., 1983) have been called into question (van der Meer, Obin, Zawistowski, Sheehan, and Richmond, 1986; Scott and Richmond, 1987) but argued by others (Ferveur, Cobb and Jallon, 1989) to still have force, at least insofar as an anti-aphrodisiac role for cis-vaccenyl acetate goes.