High impact information on Myo61F

• In the adult gut, MIA and MIB both exhibit a microvillar component as MIA attains a more apical position in addition to its previous terminal web locale [1].
• In the larval brush border, MIA is enriched in the subapical terminal web domain whereas MIB is found predominantly in the apical microvillar domain [1].
• Characterization of myosin-IA and myosin-IB, two unconventional myosins associated with the Drosophila brush border cytoskeleton [1].
• MIB is also found in egg chambers at both the basolateral and apical surfaces of the somatic follicle cells during oogenesis [1].
• MIA and MIB, both found predominantly at the basolateral domain of immature enterocytes, exhibit increased expression at the apical domain of differentiated enterocytes co-incident with microvillus assembly [1].

Biological context of Myo61F

• Amoeba genomic DNA blots probed with a short, highly conserved sequence whose position is transposed between MIB and MIL indicate that the Acanthamoeba myosin I heavy-chain gene family may actually contain as many as six genes [2].

Associations of Myo61F with chemical compounds

• Similar to the previously characterized MIB heavy-chain gene, the deduced MIL heavy-chain aa sequence reveals a 125-kDa protein composed of a myosin globular head domain joined to a novel, approx. 50-kDa C-terminal domain that is rich in glycine, proline and alanine residues [2].
• Myo1B mutant larvae also exhibit enhanced sensitivity to oral infection by the bacterial pathogen Pseudomonas entomophila, and severe cytoskeletal defects are observed in the BB of proximal midgut epithelial cells soon after infection [3].

Other interactions of Myo61F

• Overexpression of Myo61F, another myosin I (ref. 4), reverses the handedness of the embryonic gut, and its knockdown also causes a left-right patterning defect [4].
• Although both are myosins-I from fly, myosin-IA at cytological locus 31D-F and myosin-IB at cytological locus 61F appear to be more similar to their vertebrate homologs than they are to each other [5].

Analytical, diagnostic and therapeutic context of Myo61F

• Colocalization of MIA and MIB to larval and adult gut by confocal microscopy demonstrates distinct but overlapping subcellular distributions of these two proteins [1].
• Just as the sequence comparisons demonstrate a disparity between myosin-IA and myosin-IB, Northern blot analysis of these two unconventional myosins indicates distinct patterns of temporal expression [5].
• The molecular cloning and characterization of Drosophila melanogaster myosin-IA and myosin-IB [5].
• Primary sequence analyses of both the head and tail domains of the known class I myosins illustrate a division of the metazoan myosin-I family into four distinct subclasses with myosin-IA and myosin-IB as members of two of these groups [5].

References