The Myosin Va Head Domain Binds to the Neurofilament-L Rod and Modulates Endoplasmic Reticulum (ER) Content and Distribution within Axons

Rao, M. Subba; Mohan, Panaiyur S.; Kumar, Asok; Yuan, Ao; Montagna, Lee; Campbell, Jabbar; Veeranna,; Espreáfico, Enilza Maria; Julien, J.P.; Nixon, Ralph A.

doi:10.1371/journal.pone.0017087

Cited by 45 publications

(42 citation statements)

References 52 publications

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“…Myelination has an effect on NF phosphorylation. This is evidenced by the observations that NF phosphorylation is decreased in dysmyelinating mutant Trembler mice (de Waegh et al, 1992) and at the initial segment of optic nerves and nodes of Ranvier (the gaps formed between the myelin sheaths generated by different cells) (Hsieh et al, 1994;Mata et al, 1992;Reles and Friede, 1991), as well as by the possible role of myelin associated glycoprotein (MAG) as a mediator of myelin signals that alter NF phosphorylation (Dashiell et al, 2002;Yin et al, 1998). Phosphorylation of the tail domain can regulate both the interactions between the NF domains themselves and with microtubules (Hisanaga and Hirokawa, 1989;Hisanaga et al, 1991).…”

Section: Neurofilament Phosphorylationmentioning

confidence: 96%

“…A number of specific roles have been identified for the protein domains in each NF subunit, which confer to the heteropolymer (see poster panel, NF assembly) the general properties of a scaffold for the docking and organization of different axoplasmic constituents (Balastik et al, 2008;Kim et al, 2011;Rao et al, 2011). NF subunits contain a globular head, an a-helical rod domain, and variable tail domains that differ in length and amino acid composition.…”

Section: Neurofilament Structure and Functionmentioning

confidence: 99%

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Neurofilaments at a glance

Yuan

Rao

Veeranna

et al. 2012

Journal of Cell Science

351

259

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Section: Neurofilament Phosphorylationmentioning

confidence: 96%

Section: Neurofilament Structure and Functionmentioning

confidence: 99%

Neurofilaments at a glance

Yuan

Rao

Veeranna

et al. 2012

Journal of Cell Science

351

259

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“…This organization of the axonal cytoskeleton provides structural support and docking sites for reversible interactions with vesicular organelles (Steiner etal. 1987; Wagner et al 2003; Rao et al 2011) andmolecular motors (Yabe et al 1999; Shah et al 2000; Rao et al 2002a; Xia et al 2003). …”

Section: Subunit Composition Of Nfsmentioning

confidence: 99%

“…Apart from being structural elements in axons, NFs form cellular scaffolds for docking and organization of synaptic vesicles, endosomes, and the endoplasmic reticulum (ER) (Rao et al 2002a; Balastik et al 2008; Kim et al 2011; Rao et al 2011). Myosin Va in neurons binds to NF-L, and this interaction is essential for the normal distribution of ER and other organelles in the axon.…”

Section: Nf Subunit-interacting Organelles and Proteinsmentioning

confidence: 99%

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Neurofilaments and Neurofilament Proteins in Health and Disease

Yuan

Rao

Veeranna

et al. 2017

Cold Spring Harb Perspect Biol

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564

493

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SUMMARY Neurofilaments (NFs) are unique among tissue-specific classes of intermediate filaments (IFs) in being heteropolymers composed of four subunits (NF-L [neurofilament light]; NF-M [neurofilament middle];NF-H [neurofilament heavy];and α-internexin or peripherin), each having different domain structures and functions. Here, we review how NFs provide structural support for the highly asymmetric geometries of neurons and, especially, for the marked radial expansion of myelinated axons crucial for effective nerve conduction velocity. NFs in axons extensively cross-bridge and interconnect with other non-IF components of the cytoskeleton, including microtubules, actin filaments, and other fibrous cytoskeletal elements, to establish a regionally specialized network that undergoes exceptionally slow local turnover and serves as a docking platform to organize other organelles and proteins. We also discuss how a small pool of oligomeric and short filamentous precursors in the slow phase of axonal transport maintains this network. A complex pattern of phosphorylation and dephosphorylation events on each subunit modulates filament assembly, turnover, and organization within the axonal cytoskeleton. Multiple factors, and especially turnover rate, determine the size of the network, which can vary substantially along the axon. NF gene mutations cause several neuroaxonal disorders characterized by disrupted subunit assembly and NF aggregation. Additional NF alterations are associated with varied neuropsychiatric disorders. New evidence that subunits of NFs exist within postsynaptic terminal boutons and influence neurotransmission suggests how NF proteins might contribute to normal synaptic function and neuropsychiatric disease states.

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Role of myosin Va in neuritogenesis of chick dorsal root ganglia nociceptive neurons

Kanno

Espreáfico

Yan

2013

Cell Biology International

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Myosin-Va, widely distributed throughout the developing nervous system, is involved in the transport of vesicles and other intracellular components with its globular tail domain (GTD) implicated in cargo recognition/interaction. Inactivation of myosin-Va in dorsal root ganglia (DRG) neurons of chick embryos, in vitro, decreases the rate of filopodial extension. MYO5A mutant mice have severe neurological defects. We have found that the overexpression of GTD in DRG cultures reduces the number of neurons with long neurites (above fourfold cell body length) and increased the number of neurons with short or no neurites. However, if transfection occurred after the onset of neuritogenesis, this was not seen. In embryo, we characterized the expression pattern of myosin-Va during neuritogenesis of TrkA-positive cells at different stages of chick DRG development. Myosin-Va expression was detected starting from HH25. At this stage, it was present in cells both with and without neurites. The presence of myosin-Va in DRG neurites persisted throughout the last stage analysed (HH34). The data suggest that Myosin Va can participate in embryonic DRG neuritogenesis.

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The Myosin Va Head Domain Binds to the Neurofilament-L Rod and Modulates Endoplasmic Reticulum (ER) Content and Distribution within Axons

Cited by 45 publications

References 52 publications

Neurofilaments at a glance

Neurofilaments at a glance

Neurofilaments and Neurofilament Proteins in Health and Disease

Role of myosin Va in neuritogenesis of chick dorsal root ganglia nociceptive neurons

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