Myosin IIb-dependent Regulation of Actin Dynamics Is Required for N-Methyl-d-aspartate Receptor Trafficking during Synaptic Plasticity

Bu, Yun-Fei; Wang, Ning; Wang, Shaoli; Sheng, Tao; Tian, Tian; Chen, Linlin; Pan, Wei-Wei; Zhu, Min–Sheng; Luo, Jianhong; Lü, Wei

doi:10.1074/jbc.m115.644229

Cited by 15 publications

(13 citation statements)

References 59 publications

(90 reference statements)

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“…These results may not be surprising as NMHC-IIs are homologous protein molecules possibly possessing similar structural and functional features for their interaction with Na + /K + -ATPase α1 subunits although they are engaged in unique biological functions at distinct cellular locations [ 36 – 40 ]. The interaction of NMHC-IIs with Na + /K + -ATPase α1 subunits are consistent with previous findings that NMHC-IIs interact with various proteins such as C-X-C chemokine receptor type 4 (CXCR4) [ 41 ], collagen receptor DDR1 (discoidin domain receptor 1) [ 42 ], Ins (1,4,5)P 3 receptor [ 43 ], epidermal growth factor receptor (EGFR) [ 44 ], N-Methyl-d-aspartate (NMDA) receptors [ 45 ], α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor [ 46 ], the pore-forming subunit of P/Q-type calcium channels (Ca v 2.1) [ 47 ], battenin/juvenile Batten disease protein (Cln3: a lysosomal membrane protein) [ 48 ]; etc. A recent report implicates non-muscle myosin II (NM-II) in the sorting and post-Golgi dendritic trafficking of Kv2.1 channels [ 49 ].…”

Section: Discussionsupporting

confidence: 90%

Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

2018

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The alpha1 (α1) subunit of the sodium/potassium ATPase (i.e., Na+/K+-ATPase α1), the prototypical sodium pump, is expressed in each eukaryotic cell. They pump out three sodium ions in exchange for two extracellular potassium ions to establish a cellular electrochemical gradient important for firing of neuronal and cardiac action potentials. We hypothesized that myosin (myo or myh) motor proteins might interact with Na+/K+-ATPase α1 subunits in order for them to play an important role in the transport and trafficking of sodium pump. To this end immunoassays were performed to determine whether class II non-muscle myosins (i.e., NMHC-IIA/myh9, NMHC-IIB/myh10 or NMHC-IIC/myh14), myosin Va (myoVa) and myosin VI (myoVI) would interact with Na+/K+-ATPase α1 subunits. Immunoprecipitation of myh9, myh10, myh14, myoVa and myoVI from rat brain tissues led to the co-immunoprecipitation of Na+/K+-ATPase α1 subunits expressed there. Heterologous expression studies using HEK293 cells indicated that recombinant myh9, myh10, myh14 and myoVI interact with Na+/K+-ATPase α1 subunits expressed in HEK293 cells. Additional results indicated that loss of tail regions in recombinant myh9, myh10, myh14 and myoVI did not affect their interaction with Na+/K+-ATPase α1 subunits. However, recombinant myh9, myh10 and myh14 mutants having reduced or no actin binding ability, as a result of loss of their actin binding sites, displayed greatly reduced or null interaction with Na+/K+-ATPase α1 subunits. These results suggested the involvement of the actin binding site, but not tail regions, of NMHC-IIs in their interaction with Na+/K+-ATPase α1 subunits. Overall these results suggest a role for these diverse myosins in the trafficking and transport of sodium pump in neuronal and non-neuronal tissues.Electronic supplementary materialThe online version of this article (10.1186/s13041-018-0388-1) contains supplementary material, which is available to authorized users.

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Section: Discussionsupporting

confidence: 90%

Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

2018

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“…The values of the ratios were defined as [ p 2/ p 1], where p 1 and p 2 are the amplitudes of the EPSCs evoked by the first and second pulses, respectively ( 34 , 35 ). To clarify the mechanism by which GPR40 affects NMDAR surface expression levels, the exocytosis blocker TeTx (0.1 μM; Sigma-Aldrich) and the endocytosis blocker dynasore (80 mM; Abcam) were added to the internal solution for NMDA-EPSC recordings ( 45 , 46 ).…”

Section: Methodsmentioning

confidence: 99%

GPR40 modulates epileptic seizure and NMDA receptor function

Yang

Tian

et al. 2018

Sci. Adv.

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“…However, the exact proteins and mechanisms involved are still unclear. Myosin IIb has been shown to be involved in insertion of NMDARs at the membrane, but it is not believed that it is responsible for transporting it to the membrane [ 148 ]. At the surface of the synapse, NMDARs are associated with scaffolding proteins of the PSD [ 149 ].…”

Section: The Actin Cytoskeleton As Key Regulator In Glutamate Recementioning

confidence: 99%

Regulation of the Postsynaptic Compartment of Excitatory Synapses by the Actin Cytoskeleton in Health and Its Disruption in Disease

et al. 2016

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Disruption of synaptic function at excitatory synapses is one of the earliest pathological changes seen in wide range of neurological diseases. The proper control of the segregation of neurotransmitter receptors at these synapses is directly correlated with the intact regulation of the postsynaptic cytoskeleton. In this review, we are discussing key factors that regulate the structure and dynamics of the actin cytoskeleton, the major cytoskeletal building block that supports the postsynaptic compartment. Special attention is given to the complex interplay of actin-associated proteins that are found in the synaptic specialization. We then discuss our current understanding of how disruption of these cytoskeletal elements may contribute to the pathological events observed in the nervous system under disease conditions with a particular focus on Alzheimer's disease pathology.

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Myosin IIb-dependent Regulation of Actin Dynamics Is Required for N-Methyl-d-aspartate Receptor Trafficking during Synaptic Plasticity

Cited by 15 publications

References 59 publications

Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

GPR40 modulates epileptic seizure and NMDA receptor function

Regulation of the Postsynaptic Compartment of Excitatory Synapses by the Actin Cytoskeleton in Health and Its Disruption in Disease

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