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Volumn 10, Issue 1, 1998, Pages 80-86

Myosins: Matching functions with motors

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MYOSIN;

EID: 0032005265     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80089-6     Document Type: Article
Times cited : (66)

References (52)
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    • of outstanding interest. Early investigators postulated that the mouse dilute phenotype was due to the improper outgrowth of dendritic melanocyte spines. The authors of this paper isolated dilute melanocytes and showed that they were still dendritic, but that the melanosomes failed to migrate into the arbors.
    • Provance DW Jr, Wei M, Ipe V, Mercer JA. Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution. of outstanding interest Proc Natl Acad Sci USA. 93:1996;14554-14558 Early investigators postulated that the mouse dilute phenotype was due to the improper outgrowth of dendritic melanocyte spines. The authors of this paper isolated dilute melanocytes and showed that they were still dendritic, but that the melanosomes failed to migrate into the arbors.
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    • of outstanding interest. Immunofluorescent and immunoelectron microscopy were utilized to explore the in vivo association of myosin V with melanosomes. The results of this paper point to both actin- and microtubule-dependent motility of these organelles. The acto-myosin driven segment appears to be in the dendritic endings alone.
    • Wu X, Bowers B, Wei Q, Kocher B, Hammer JA III. Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. of outstanding interest J Cell Sci. 110:1997;847-859 Immunofluorescent and immunoelectron microscopy were utilized to explore the in vivo association of myosin V with melanosomes. The results of this paper point to both actin- and microtubule-dependent motility of these organelles. The acto-myosin driven segment appears to be in the dendritic endings alone.
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    • The predominant defect in dilute melanocytes is in melanosome distribution and not cell shape, supporting a role for myosin V in melanosome transport
    • of special interest. These authors also explore the morphology of mouse dilute melanocytes and demonstrate that these cells are still dendritic, but the melanosomes fail to migrate into the arbors both in vitro and in situ.
    • Wei Q, Wu X, Hammer JA III. The predominant defect in dilute melanocytes is in melanosome distribution and not cell shape, supporting a role for myosin V in melanosome transport. of special interest J Mus Res Cell Motil. 18:1997;517-527 These authors also explore the morphology of mouse dilute melanocytes and demonstrate that these cells are still dendritic, but the melanosomes fail to migrate into the arbors both in vitro and in situ.
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    • of outstanding interest. A beautiful study of myosin V localization in superior cervical ganglion neurons. Myosin V is enriched in organelle-rich zones of the extended growth cone and associated with a distinct subset of small organelles which are themselves associated with both actin and microtubules. The authors also explore the hypothesis that structural abnormalities in the mouse dilute neurons could account for neurological dysfunction. The morphology of the dilute-lethal neurons appears to be normal. These results are somewhat in conflict with earlier analyses that suggested that myosin V was required for neuronal extension; however, they might be reconciled with earlier studies if a different myosin V compensates for the loss of the dilute protein during neuronal growth and development.
    • Evans LL, Hammer J, Bridgman PC. Subcellular localization of myosin V in nerve growth cones and outgrowth from dilute-lethal neurons. of outstanding interest J Cell Sci. 110:1997;439-449 A beautiful study of myosin V localization in superior cervical ganglion neurons. Myosin V is enriched in organelle-rich zones of the extended growth cone and associated with a distinct subset of small organelles which are themselves associated with both actin and microtubules. The authors also explore the hypothesis that structural abnormalities in the mouse dilute neurons could account for neurological dysfunction. The morphology of the dilute-lethal neurons appears to be normal. These results are somewhat in conflict with earlier analyses that suggested that myosin V was required for neuronal extension; however, they might be reconciled with earlier studies if a different myosin V compensates for the loss of the dilute protein during neuronal growth and development.
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    • of outstanding interest. A study examining the association of myosin V with organelles in the cultured melanocyte. Immunolocalization results demonstrate that myosin V colocalizes with melanosomes as well as other membrane-bound organelles. Subcellular fractionation experiments reveal that myosin V cofractionates with melanosomes. Treatment of cells with serotonin to stimulate melanin synthesis (and production of melanosomes) results in increased levels of myosin V present in the cell.
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    • of outstanding interest. The authors present biochemical data demonstrating a functional association of myosin V with synaptic vesicles. They also show that myosin V is associated with the synaptobrevin/synaptophysin complex. They suggest that myosin V may play an important role in the transport of synaptobrevin/synaptophysin-containing vesicles in nerve terminals.
    • 2+-dependent interaction with the snaptobrevin-synaptophysin complex. of outstanding interest J Cell Biol. 137:1997;1589-1601 The authors present biochemical data demonstrating a functional association of myosin V with synaptic vesicles. They also show that myosin V is associated with the synaptobrevin/synaptophysin complex. They suggest that myosin V may play an important role in the transport of synaptobrevin/synaptophysin-containing vesicles in nerve terminals.
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    • of special interest. The origin of the neurological disorders in dilute mice is unknown. The brains appear normal at the gross level. These authors carried out a morphological analysis of the brains of dilute-lethal mice and found that the smooth endoplasmic reticulum of dilute mice was incorrectly localized and did not extend into the dendritic spines of Purkinje cells. The mislocation of the smooth ER may contribute to neurological dysfunction in these mice.
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    • of special interest. Myosin V is thought to act in trafficking of membrane-bound organelles. Further support for this hypothesis is provided by this analysis of the inheritance of the yeast vacuole. The yeast myo2 mutants were shown to fail to efficiently move the vacuole into their daughter cells. The authors find that Myop is localized to the vacuole and the tip of the growing bud (where the vacuole is anchored in wild type cells).
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    • Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p
    • of special interest. Yet another interesting function for myosin V in yeast. This time for the first myosin V identified, myo2. This paper presents data showing that myosin V mutants fail to properly localize a chitin synthase in cells about to divide. This chitin synthase is crucial for determining the position of the daughter cell bud.
    • Santos B, Snyder M. Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p. of special interest J Cell Biol. 136:1997;95-110 Yet another interesting function for myosin V in yeast. This time for the first myosin V identified, myo2. This paper presents data showing that myosin V mutants fail to properly localize a chitin synthase in cells about to divide. This chitin synthase is crucial for determining the position of the daughter cell bud.
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    • of special interest. The authors devised a clever screen to identify genes required for the suppression of mating type switching in the yeast daughter cell. They identified several genes essential for this process, one of which encodes the second yeast myosin V, Myo4p.
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    • Asymmetric accumulation of Ash1p in post-anaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells
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    • Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast
    • of outstanding interest. There is a more interesting twist to the Myo4p story than originally thought. myo4 mutants fail to properly localize the Ash1 mRNA to the tip of the growing bud. A similar erffect is observed upon isruption of the actin cytoskeleton.
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    • Mating type switching in yeast controlled by asymmetric localization of ash1 mrna
    • of outstanding interest. These authors also show that myo4 mutants fail to properly localize the Ash1 message to the daughter cell. This suggests that myosin V may not simply act as an organelle motor but may participate in the localization of mRNAs as well.
    • Long RM, Singer RH, Meng XH, Gonzalez I, Nasmyth K, Jansen RP. Mating type switching in yeast controlled by asymmetric localization of ash1 mrna. of outstanding interest Science. 277:1997;383-387 These authors also show that myo4 mutants fail to properly localize the Ash1 message to the daughter cell. This suggests that myosin V may not simply act as an organelle motor but may participate in the localization of mRNAs as well.
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    • Long, R.M.1    Singer, R.H.2    Meng, X.H.3    Gonzalez, I.4    Nasmyth, K.5    Jansen, R.P.6
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    • A non-muscle myosin required for embryonic polarity in Caenorhabditis elegans
    • of outstanding interest. A surprising result from this lab showed a non-muscle myosin II to be involved in correct asymmetric partitioning in Caenorhabditis elegans. It was found that this protein is coprecipitated with another protein involved in this process, Par-1.
    • Guo S, Kemphues KJ. A non-muscle myosin required for embryonic polarity in Caenorhabditis elegans. of outstanding interest Nature. 382:1996;455-458 A surprising result from this lab showed a non-muscle myosin II to be involved in correct asymmetric partitioning in Caenorhabditis elegans. It was found that this protein is coprecipitated with another protein involved in this process, Par-1.
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    • A Dictyostelium myosin I plays a crucial role in regulating the frequency of pseudopods formed on the substratum
    • of special interest. The original data on myosin I in Dictyostelium showed that deletion of these genes reduced the instantaneous velocity of these cells. This paper shows that this is probably due to excess turning which is the result of too many pseudopods being produced adjacent to the substratum. This points to a role for this class in suppression of membrane extensions.
    • Wessels D, Titus MA, Soll DR. A Dictyostelium myosin I plays a crucial role in regulating the frequency of pseudopods formed on the substratum. of special interest Cell Motil Cytoskeleton. 33:1996;64-79 The original data on myosin I in Dictyostelium showed that deletion of these genes reduced the instantaneous velocity of these cells. This paper shows that this is probably due to excess turning which is the result of too many pseudopods being produced adjacent to the substratum. This points to a role for this class in suppression of membrane extensions.
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    • Function of myosin-V in filopodial extension of neuronal growth cones
    • of special interest. A novel method of studying myosin function using microCALI. These authors attach a light sensitive probe to a specific antibody. When this probe is irradiated, it becomes toxic to proteins attached to the antibody. This allows study in small areas and short time scales. The authors use this to inhibit both myosin I and myosin V in growth cones.
    • Wang FS, Wolenski JS, Cheney RE, Mooseker MS, Jay DG. Function of myosin-V in filopodial extension of neuronal growth cones. of special interest Science. 273:1996;660-663 A novel method of studying myosin function using microCALI. These authors attach a light sensitive probe to a specific antibody. When this probe is irradiated, it becomes toxic to proteins attached to the antibody. This allows study in small areas and short time scales. The authors use this to inhibit both myosin I and myosin V in growth cones.
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