Interaction domains of neurofilament light chain and brain spectrin

Frappier, Thierry; Stetzkowski‐Marden, Françoise; Pradel, Louise‐Anne

doi:10.1042/bj2750521

Cited by 50 publications

(32 citation statements)

References 51 publications

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“…Recent observations identify NFs as a major ligand of myosin in situ (Rao et al, 2002). NFs also have been shown to bind the actin-associated protein spectrin (Frappier et al, 1987(Frappier et al, , 1991. These observations, coupled with the observation that some NFs and punctate structures containing NF subunits translocate along the peripheral area of axonal neurites (Yabe et al, 2001a,b), leave open the possibility that the submembrane actin cortex and/or its associated motor myosin may facilitate axonal transport of NFs.…”

Section: Introductionmentioning

confidence: 88%

Neurofilament Transport Is Dependent on Actin and Myosin

Jung¹,

Chylinski²,

Pimenta³

et al. 2004

J. Neurosci.

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Real-time analyses have revealed that some newly synthesized neurofilament (NF) subunits translocate into and along axonal neurites by moving along the inner plasma membrane surface, suggesting that they may translocate against the submembrane actin cortex. We therefore examined whether or not NF axonal transport was dependent on actin and myosin. Perturbation of filamentous actin in NB2a/d1 cells with cytochalasin B inhibited translocation of subunits into axonal neurites and inhibited bidirectional translocation of NF subunits within neurites. Intravitreal injection of cytochalasin B inhibited NF axonal transport in optic axons in a dose-response manner. NF subunits were coprecipitated from NB2a/d1 cells by an anti-myosin antibody, and myosin colocalized with NFs in immunofluorescent analyses. The myosin light chain kinase inhibitor ML-7 and the myosin ATPase inhibitor 2,3-butanedione-2-monoxime perturbed NF translocation within NB2a/d1 axonal neurites. These findings suggest that some NF subunits may undergo axonal transport via myosinmediated interactions with the actin cortex.

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Section: Introductionmentioning

confidence: 88%

Neurofilament Transport Is Dependent on Actin and Myosin

Jung¹,

Chylinski²,

Pimenta³

et al. 2004

J. Neurosci.

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“…Although it is tempting to speculate that desmin IFs anchor to ␣-fodrin at the sarcolemma at Z line domains, binding of desmin to ␣ subunits of the spectrin superfamily has yet to be reported. Desmin and other IF proteins bind to spectrin and to ankyrin (Georgatos and Blobel, 1987;Langley and Cohen, 1987;Frappier et al, 1991Frappier et al, , 1992Macioce et al, 1999), however, so anchoring of desmin IFs to the sarcolemma may be mediated by the ␣␤-spectrin heteromers and ankyrin that are present at Z line domains (Porter et al, 1997;Williams and Bloch, 1999b;Williams et al, 2001; see Figure 9). …”

Section: Discussionmentioning

confidence: 99%

Sarcolemmal Organization in Skeletal Muscle Lacking Desmin: Evidence for Cytokeratins Associated with the Membrane Skeleton at Costameres

O’Neill

Williams

Resneck

et al. 2002

MBoC

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The sarcolemma of fast-twitch muscle is organized into "costameres," structures that are oriented transversely, over the Z and M lines of nearby myofibrils, and longitudinally, to form a rectilinear lattice. Here we examine the role of desmin, the major intermediate filament protein of muscle in organizing costameres. In control mouse muscle, desmin is enriched at the sarcolemmal domains that lie over nearby Z lines and that also contain ␤-spectrin. In tibialis anterior muscle from mice lacking desmin due to homologous recombination, most costameres are lost. In myofibers from desmin Ϫ/Ϫ quadriceps, by contrast, most costameric structures are stable. Alternatively, Z line domains may be lost, whereas domains oriented longitudinally or lying over M lines are retained. Experiments with pan-specific antibodies to intermediate filament proteins and to cytokeratins suggest that control and desmin Ϫ/Ϫ muscles express similar levels of cytokeratins. Cytokeratins concentrate at the sarcolemma at all three domains of costameres when the latter are retained in desmin Ϫ/Ϫ muscle and redistribute with ␤-spectrin at the sarcolemma when costameres are lost. Our results suggest that desmin associates with and selectively stabilizes the Z line domains of costameres, but that cytokeratins associate with all three domains of costameres, even in the absence of desmin. INTRODUCTIONDuchenne Muscular Dystrophy and related muscular dystrophies are caused by the mutation or loss of dystrophin and dystrophin-associated proteins (Campbell, 1995;Bonnemann et al., 1996;Straub and Campbell, 1997;Ozawa et al., 1998), respectively, but the functions of these proteins in healthy skeletal muscle are still poorly understood. Dystrophin, which is a member of the spectrin superfamily of membrane skeletal proteins (Davison and Critchley, 1988;Koenig et al., 1988;Dhermy, 1991;Ahn and Kunkel, 1993), accumulates in healthy muscle on the cytoplasmic face of the sarcolemma in linear structures that are oriented both longitudinally and transversely (Masuda et al., 1992;Minetti et al., 1992;Porter et al., 1992;Straub et al., 1992;Williams and Bloch, 1999b). The transverse structures, which lie at the sarcolemma over the Z and M lines of nearby myofibrils, are organized in a rib-like pattern and so are referred to as "costameres" (Pardo et al., 1983a). We also use this term to include the longitudinal elements, which, with the transverse domains, form a lattice-like network that underlies most of the skeletal muscle sarcolemma. All three costameric domains are enriched in dystrophin (Porter et al., 1992). We have found that, in the absence of dystrophin, the longitudinal and M line domains of costameres are more susceptible to disruption in Duchenne muscle and in muscle from the mdx mouse (Porter et al., 1992;Williams and Bloch, 1999b; see also Ehmer et al., 1997), suggesting that dystrophin functions more to stabilize these sarcolemmal domains than the domains that overlie Z lines. These studies also suggest that other structures associated with the sarco...

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“…Certain of these sites completely turn over their phosphates in vivo without hours after synthesis, before neurofilaments have moved a considerable distance into the axon [Sihag and Nixon, 1989, 19911. It seems likely that some head domain sites are binding sites for other proteins, although none has yet been reported, and, remarkably, most of the binding sites for cytoskeletal proteins have so far been found on NF-L [Frappier et al, 1987[Frappier et al, , 1991Heimann et al, 1985;Miyata et al, 19861. Another possible function of NF-M head domain sites regulated by second messenger-dependent kinases may be to stabilize the assembled state of the neurofilament and to reduce its sensitivity to phosphorylation-induced disassembly [Nixon and Sihag, 19911-a property that may be disadvantageous to the long-lived filaments that support the axon.…”

Section: Neurofilament Dynamicsmentioning

confidence: 99%