title: Subcellular localization of PMES-2 proteins regulated by their two cytoskeleton-associated domains.
abstract: 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. 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. This dual-targeting of PMES-2 constructs depends on an effector domain-like motif in the N-terminus. 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.
authors.affiliation: Research Institute for Cell Engineering (RICE), National Institute of Advanced Industrial Science and Technology (AIST), 1-8-31 Midorigaoka, Ikeda, Osaka, 563-8577, Japan.
authors.forename: Kensuke
authors.initials: K
authors.lastname: Ninomiya
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Ishimoto
authors.forename: Takahisa
authors.initials: T
authors.lastname: Taguchi
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D003593:Cytoplasm / Q000378:metabolism; D019922:GAP-43 Protein / Q000737:chemistry / Q000235:genetics; D006624:Hippocampus / Q000166:cytology; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry / Q000235:genetics; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D016501:Neurites / Q000378:metabolism*; D009474:Neurons / Q000378:metabolism / Q000648:ultrastructure; D017434:Protein Structure, Tertiary; D051381:Rats; D017207:Rats, Sprague-Dawley; D013569:Synapses / Q000378:metabolism; D014162:Transfection; D020798:Two-Hybrid System Techniques
chemical_list: C470839:Bcas1 protein, rat; D019922:GAP-43 Protein; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate