Endoplasmic reticulum is missing in dendritic spines of Purkinje cells of the ataxic mutant rat

Dekker-Ohno, K.; Hayasaka, Shizu; Takagishi, Yoshiko; Oda, Sen-ichi; Wakasugi, Noboru; Mikoshiba, Katsuhiko; Inouye, Minoru; Yamamura, Hideki

doi:10.1016/0006-8993(95)01560-4

Cited by 88 publications

(57 citation statements)

References 17 publications

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“…The yeast two-hybrid studies suggest that one way this transport is coordinated is through the direct interaction of the different motor molecules. These data are consistent with previous studies, which showed that MyoVa and kinesin both can bind synaptic vesicles in the rat (17,18) and that MyoVa is required for short-range, but not long-range, transport of smooth endoplasmic reticulum in Purkinje cells (9,10).…”

supporting

confidence: 93%

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A mutation in Rab27a causes the vesicle transport defects observed in ashen mice

Wilson

Yip

Swing

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

381

363

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The dilute (d), leaden (ln), and ashen (ash) mutations provide a unique model system for studying vesicle transport in mammals. All three mutations produce a lightened coat color because of defects in pigment granule transport. In addition, all three mutations are suppressed by the semidominant dilute-suppressor (dsu), providing genetic evidence that these mutations function in the same or overlapping transport pathways. Previous studies showed that d encodes a major vesicle transport motor, myosin-VA, which is mutated in Griscelli syndrome patients. Here, using positional cloning and bacterial artificial chromosome rescue, we show that ash encodes Rab27a. Rab GTPases represent the largest branch of the p21 Ras superfamily and are recognized as key players in vesicular transport and organelle dynamics in eukaryotic cells. We also show that ash mice have platelet defects resulting in increased bleeding times and a reduction in the number of platelet dense granules. These defects have not been reported for d and ln mice. Collectively, our studies identify Rab27a as a critical gene for organelle-specific protein trafficking in melanocytes and platelets and suggest that Rab27a functions in both MyoVa dependent and independent pathways.

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supporting

confidence: 93%

“…The neurological defect is thought to result from the failure to transport smooth endoplasmic reticulum (SER) from the dendritic shaft to the dendritic spines of cerebellar Purkinje cells (9,10). The absence of SER in spines probably disrupts the regulation of intracellular Ca 2ϩ and postsynaptic signal transduction.…”

mentioning

confidence: 99%

A mutation in Rab27a causes the vesicle transport defects observed in ashen mice

Wilson

Yip

Swing

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

381

363

View full text Add to dashboard Cite

show abstract

“…In yeast, it is well-established that a member of the myosin-V family, Myo4p, transports Ash-1 mRNA [Takizawa et al, 1997;Beach and Bloom, 2001;Muller et al, 2007]. Therefore, an RNA transport/tethering deficit in Myo5a null mutant mice may be sufficient to cause the physiological Miyata et al, 2000] and morphological [Dekker-Ohno et al, 1996;Takagishi et al, 2007] phenotypes observed in the central nervous system. Circumstantial evidence suggesting a role for myosinVa in RNA transport in vertebrate neurons was first published in 2002 [Ohashi et al, 2002], but identification of a specific message associated with myosin-Va, Nd1-L, was only recently published [Yoshimura et al, 2006].…”

Section: Discussionmentioning

confidence: 99%

“…Endoplasmic reticulum is missing in dendritic spines of cerebellar Purkinje cells [Dekker-Ohno et al, 1996;Takagishi et al, 1996] from null mutant rats, long-term synaptic depression (LTD) is abolished in null mutant mice [Miyata et al, 2000], and antibody inhibition of myosin Va causes a delay in neurotransmitter release [Rosé et al, 2003]. While these differences can explain the neurological phenotype, a clear pathway has yet to be demonstrated.…”

Section: Introductionmentioning

confidence: 99%

Myosin‐Va mediates RNA distribution in primary fibroblasts from multiple organs

Salerno

Calliari

Provance

et al. 2008

Cell Motil. Cytoskeleton

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Myosin-Va has been shown to have multiple functions in a variety of cell types, including a role in RNA transport in neurons. Using primary cultures of cells from organs of young dilute-lethal (Myo5a d-l /Myo5a d-l ) null mutant mice and wild-type controls, we show that in some, but not all, tissues, RNA distribution is dramatically different in the homozygous null mutant cells. The dependence of RNA localization on myosin-Va correlates with the relative abundance of the brainspecific splicing pattern of the myosin-Va tail. We also show that myosin-Va is involved in RNA localization soon after synthesis, because the effects of its absence are diminished for RNAs that are more than 30 min old. Finally, we show that localization of β-actin mRNA is significantly changed by the absence of myosin-Va. These results suggest that myosin-Va is involved in a transient transport or tethering function in the perinuclear region. Cell Motil.

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“…The specific dysfunction that leads to the convulsions and post-natal death in these animals is not known. However, recent evidence has implicated MVa in several neuronal processes, including its binding to synaptic vesicle associated proteins (Prekeris and Terrian, 1997;Costa et al, 1999;Ohyama et al, 2001), its association with organelle and vesicle movement within axons (Evans et al, 1998;Tabb et al, 1998) as well as its critical role in the localization of smooth endoplasmic reticulum in dendritic spines of Purkinje cells (Dekker-Ohno et al, 1996). The subcellular localization of MVa has been described in neuronal and glial cells by immunoprobes and shows a characteristic punctate labeling, frequently being concentrated at the neurite tips and growth cones, as well as at the perinuclear region .…”

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confidence: 99%

Immunohistochemical localization of myosin va in the adult rat brain

et al. 2003

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Abstract-Brain myosin Va (MVa) is a molecular motor associated with plastic changes during development. MVa has previously been detected in the cell body and in dendrites of neuronal cells in culture, in cells of the guinea-pig cochlea, as well as in cerebellar cells. Adult Wistar rats (n‫,)41؍‬ 250 -300 g, were perfused with standard methods for immunohistochemistry, using a polyclonal, affinity-purified rabbit antibody against MVa tail domain. Anti-MVa antibody specifically stained neuronal nuclei from forebrain to cerebellar regions, and more intensely sensory nuclei. Differences in MVa immunoreactivity were detected between brain nuclei, ranging from very intense to weak staining. The analysis of MVa and glial fibrillary acidic protein staining in adjacent brain sections demonstrated a clear-cut neuronal labeling rather than an astroglial staining. The studies presented here represent a comprehensive map of MVa regional distribution in the CNS of the adult rat and may contribute to the basic understanding of its role in brain function and plasticity, particularly in relationship to phenomena that involve molecular motors, such as neurite outgrowth, organelle transport and neurotransmitter-vesicle cycling. It is important to highlight that this is a pioneer immunohistochemical study on the distribution of MVa on the whole brain of adult rats, a first step toward the understanding of its function in the CNS.

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Endoplasmic reticulum is missing in dendritic spines of Purkinje cells of the ataxic mutant rat

Cited by 88 publications

References 17 publications

A mutation in Rab27a causes the vesicle transport defects observed in ashen mice

A mutation in Rab27a causes the vesicle transport defects observed in ashen mice

Myosin‐Va mediates RNA distribution in primary fibroblasts from multiple organs

Immunohistochemical localization of myosin va in the adult rat brain

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