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Subcellular Localization of PMES-2 Proteins Regulated by Their two Cytoskeleton-Associated Domains

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Summary

  1. 1.

    PMES-2 is a protein, of which mRNA is translocated to the neurites of hippocampal neurons. Since the protein is present in the postsynaptic density, contributions to synaptic function have been predicted.

  2. 2.

    To elucidate the protein–protein interaction of PMES-2, yeast two-hybrid screening was performed with PMES-2 partial polypeptides as baits. We found that PMES-2 interacted with dynein light chain-2 (DLC-2), a light chain subunit of myosin-V and cytoplasmic dynein, via the C-terminal 20 amino acids. Exogenous PMES-2 colocalized with F-actin at the cell periphery, while a PMES-2 mutant lacking the DLC-binding site localized primarily in the nucleus.

  3. 3.

    This dual-targeting of PMES-2 constructs depends on an effector domain-like motif in the N-terminus.

  4. 4.

    These results indicate that PMES-2 links a motor complex to the membrane skeleton and that DLC-1/2 inhibits PMES-2 nuclear localization. PMES-2 possibly modifies the cytoskeletal architecture and protein transport at the synapse and/or regulates signal transduction from the synapse to the nucleus.

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Abbreviations

CaMK2α:

calcium/calmodulin-dependent kinase 2 α subunit

DLC:

dynein light chain

EGFP:

enhanced green fluorescent protein

GAL4-AD:

GAL4-activating domain

GAL4-DB:

GAL4-DNA binding domain

GAP-43:

growth-associated protein-43

ED:

effector domain

GKAP:

guanylate kinase-associated protein

MAP2:

microtubule-associated protein-2

MARCKS:

myristoylated alanin-rich C-kinase substrate

NABC1:

novel amplified in breast carcinoma 1

nNOS:

neuronal nitric oxide synthase

PIN:

protein inhibitor of neuronal nitric oxide synthase

PMES-2:

protein whose mRNA is enriched in synaptosomes 2

SIAH:

seven in absentia homolog

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Correspondence to Takahisa Taguchi.

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Ninomiya, K., Ishimoto, T. & Taguchi, T. Subcellular Localization of PMES-2 Proteins Regulated by Their two Cytoskeleton-Associated Domains. Cell Mol Neurobiol 25, 899–911 (2005). https://doi.org/10.1007/s10571-005-4955-5

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  • DOI: https://doi.org/10.1007/s10571-005-4955-5

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