Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization

Miller, Mark S.; Bower, E.; Levitt, Pat; Li, Deqin; Chantler, Peter D.

doi:10.1016/0896-6273(92)90106-n

Cited by 93 publications

(70 citation statements)

References 59 publications

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“…Furthermore, brain myosin has been shown to produce very dense characteristic superprecipitates on incubation with actin and Ca2+ -calmodulin-dependent myosin light-chain kinase [ll, 251. The non-muscle myosins consisting of NM1 or NM2 may thus be likely to be involved in some motility processes which are distinct from those the myosins consisting of NM3 or NM-3-like MHC are involved in, such as the particular neuronal motility processes of extension and maintenance of the axons and dendrites [27].…”

Section: Hbmmentioning

confidence: 99%

Heavy‐chain isoforms of non‐muscle myosin in human tissues

Kimura

Nakashima

Uda

et al. 1993

European Journal of Biochemistry

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The heavy-chain isoforms of myosin in human non-muscle and smooth muscle tissues were analyzed by means of SDSPAGE and using three distinct newly developed monoclonal anti-(human cerebrum myosin) Ig (HBM-1, HBM-3 and HBM-4). Purified cerebrum myosin contained three electrophoretic variants of non-muscle myosin heavy chain (NM1, NM2 and NM3, with apparent molecular masses of about 200,198 and 196 kDa, respectively). Both NM1 and NM2 were recognizable by the brain-specific antibody HBM-1, while NM3 was recognizable by HBM-3. Each of the variants reacted with HBM-4 to a similar extent. Purified cerebellum myosin gave three electrophoretic variants of the heavy chain which were indistinguishable electrophoretically or immunologically from those of cerebrum myosin. Aortic myosin contained four electrophoretic variants, including the two smooth muscle myosin heavy chain isoforms and NM2-like and NM3-like heavy chains. Liver, platelet and kidney myosins contained a heavy chain very similar to NM3. Kidney myosin also contained a small fraction of an NM2-like electrophoretic variant. In addition, cerebrum, kidney, liver and platelet myosins appeared to contain minor, 194-kDa myosin heavy-chain-like polypeptide(s) (NM4). NM1, as well as NM2 and NM3, thus appear to be the brain-type and non-braintype non-muscle myosin heavy-chain isoforms, respectively, and additional minor heavy-chain isoforms are also likely to be present in human tissues.Two cDNA clones, each encoding similar parts of two distinct non-muscle myosin heavy chains (MHC j have been isolated from a chicken fibroblast cDNA library [I], and cDNA clones encoding the entire length of one of the heavy chains were also isolated from a chicken intestinal epithelial cell cDNA library [2]. Since RNA-blot analysis revealed that the two heavy chain mRNA species, MHC-B and MHC-A, were expressed selectively in the brain and non-brain tissues, respectively, these mRNA species were proposed to encode brain-type and non-brain type MHC, respectively, while the kidney, a non-brain tissue, was found to express similar levels of the two RNA species [3]. The 198-kDa and 196-kDa MHC in chicken brain and non-brain tissues are proposed to be encoded by MHC-B and MHC-A, respectively [3].Purified bovine cerebrum myosin was shown to contain similar levels of two electrophoretic variants of the heavy chain, which were distinguishable from each other by brainspecific and non-brain-specific monoclonal anti-myosin IgG (BM-1 and BM-3, respectively), suggesting the presence of brain-specific and non-brain specific MHC isoforms in mammalian brain [4]. Similarly, a polyclonal antibody raised against a synthetic octapeptide with the sequence found in , as well as a polyclonal anti-(human platelet myosin) IgG, revealed the presence of another electrophoretic variant of the heavy chain (MIIA) in the same extracts, suggesting that brain extracts contain two brain-type MHC and a non-braintype MHC [6]. Another study using a rat cDNA probe (C4) has revealed the presence of an MHC mRNA expressed excl...

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Section: Hbmmentioning

confidence: 99%

Heavy‐chain isoforms of non‐muscle myosin in human tissues

Kimura

Nakashima

Uda

et al. 1993

European Journal of Biochemistry

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“…To understand the cellular mechanism by which NMII regulates axon growth, we first examined the localization of NMII isoforms in the growth cone. Distribution of NMII in the growth cone has been examined by several groups, reporting NMIIB in the growth cone periphery (29,30) or in the central and the transitional domains (17,26). When neurons were simultaneously fixed and detergentextracted to remove soluble proteins, we observed a clear band of NMIIB remaining bound specifically in the transitional domain of the growth cone, colocalizing with the actin arc structure (Fig.…”

Section: Nmii Inhibition Promotes Axon Growth Over Cspgs Via Reorganiza-mentioning

confidence: 99%

Engineering neuronal growth cones to promote axon regeneration over inhibitory molecules

Hur¹,

Yang²,

Kim³

et al. 2011

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

134

155

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Neurons in the central nervous system (CNS) fail to regenerate axons after injuries due to the diminished intrinsic axon growth capacity of mature neurons and the hostile extrinsic environment composed of a milieu of inhibitory factors. Recent studies revealed that targeting a particular group of extracellular inhibitory factors is insufficient to trigger long-distance axon regeneration. Instead of antagonizing the growing list of impediments, tackling a common target that mediates axon growth inhibition offers an alternative strategy to promote axon regeneration. Neuronal growth cone, the machinery that derives axon extension, is the final converging target of most, if not all, growth impediments in the CNS. In this study, we aim to promote axon growth by directly targeting the growth cone. Here we report that pharmacological inhibition or genetic silencing of nonmuscle myosin II (NMII) markedly accelerates axon growth over permissive and nonpermissive substrates, including major CNS inhibitors such as chondroitin sulfate proteoglycans and myelin-associated inhibitors. We find that NMII inhibition leads to the reorganization of both actin and microtubules (MTs) in the growth cone, resulting in MT reorganization that allows rapid axon extension over inhibitory substrates. In addition to enhancing axon extension, we show that local blockade of NMII activity in axons is sufficient to trigger axons to grow across the permissive-inhibitory border. Together, our study proposes NMII and growth cone cytoskeletal components as effective targets for promoting axon regeneration.myelin | glial scar | multi-compartment neuronal culture chamber

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“…Cell migration, neurite outgrowth, and vesicular transport are all processes that might involve myosin I's (Mitchison and Kirschner, 1988;Smith, 1988;Pollard et al, 1991) and that are central to neuronal development. Myosin I-like proteins have been localized to growth cones by immunostaining of a neuronal cell line (Miller et al, 1992) and by immunoblotting of fractions enriched in growth cone membranes (Phelan et al, 1991). To begin to address the is-…”

mentioning

confidence: 99%

Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes of the myosin I family.

Sherr

Joyce

Greene

1993

The Journal of Cell Biology

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Abstract. A polymerase chain reaction strategy was devised to identify new members of the mammalian myosin I family of actin-based motors. Using cellular RNA from mouse granular neurons and PC12 cells, we have cloned and sequenced three 1.2-kb polymerase chain reaction products that correspond to novel mammalian myosin I genes designated MMIoe, MMI~, MMI3,. The pattern of expression for each of the myosin I's is unique: messages are detected in diverse tissues including the brain, lung, kidney, liver, intestine, and adrenal gland. Overlapping clones representing full-length cDNAs for MMIc~ were obtained from mouse brain. These encode a 1,079 amino acid protein containing a myosin head, a domain with five calmodulin binding sites, and a positively charged COOH-terminal tail. In situ hybridization reveals that MMIot is highly expressed in virtually all neurons (but not glia) in the postnatal and adult mouse brain and in neuroblasts of the cerebellar external granular layer. Expression varies in different brain regions and undergoes developmental regulation. Myosin rs are present in diverse organisms from protozoa to vertebrates. This and the expression of three novel members of this family in brain and other mammalian tissues suggests that they may participate in critical and fundamental cellular processes.

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Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization

Cited by 93 publications

References 59 publications

Heavy‐chain isoforms of non‐muscle myosin in human tissues

Heavy‐chain isoforms of non‐muscle myosin in human tissues

Engineering neuronal growth cones to promote axon regeneration over inhibitory molecules

Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes of the myosin I family.

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