Nonmuscle myosin appears to be responsible for cellularization. Required for morphogenesis and cytokinesis (PubMed:24786584). Necessary for auditory transduction: plays a role in Johnston's organ organization by acting in scolopidial apical attachment (PubMed:27331610). Interaction with the myosin ck may be important for this function (PubMed:27331610). Localizes to and defines the trailing edge of cells during larval epidermal wound healing (PubMed:31704968). This process is dependent on the phosphatidylinositol 4-phosphate 5-kinase sktl/skittles (PubMed:31704968).

(UniProt, Q99323)

Encodes a 205 kilodalton myosin heavy chain found in Drosophila cell lines and all Drosophila developmental stages. Antibodies raised against this protein crossreact, but weakly with muscle myosin heavy chain. First appears in preblastoderm embryos; diffusely distributed until syncytial blastoderm at which time localization to cortex and pole cells observed; at cleavage furrow, canals at the time of cellularization; transiently present at points of invagination during gastrulation (Young et al., 1987, 1991).

The wild-type allele of zipper is expressed in the nervous system during development and was believed to encode an integral membrane protein necessary for normal axon patterning (Zhao et al., 1988); however it has more recently been shown to encode the heavy chain of cytoplasmic myosin (Kierhart). The mutants are embryonic lethals; abnormalities include a small hole in the ventral thorax, distortion of ventral denticle rows, and defects in head involution and dorsal closure (Nusslein-Volhard et al., 1984; Cote et al., 1987). These defects vary in different alleles and in different embryos from the same egg laying (Cote et al., 1987). The nervous system of mutant embryos also differentiates abnormally, showing local defects in the fasciculation pattern of axons (Zhao et al., 1988), as indicated by antibody stains for neurons and their axons. These CNS abnormalities can be detected after germ band shortening and, together with the molecular data, suggested that neurological rather than epidermal defects are the primary ones in zip mutants (Cote et al., 1987).