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Research article summary:
Targeting protein phosphatase 1 (PP1) to the actin cytoskeleton: the neurabin I/PP1 complex regulates cell morphology.
Abstract Extract:
Neurabin I, a neuronal actin-binding protein, binds protein phosphatase 1 (PP1) and p70 ribosomal S6 protein kinase (p70S6K), both proteins implicated in cytoskeletal dynamics. We expressed wild-type and mutant neurabins fused to green fluorescent ... (Full abstract text below) Published 2002Jul
in Journal: Mol Cell Biol
(Language : eng)
Full Pubmed Extract
This information was retrieved, real-time, on your behalf from the public area of the Pubmed website:
1. Mol Cell Biol.
2002 Jul;22(13):4690-701
Targeting protein phosphatase 1 (PP1) to the actin cytoskeleton: the neurabin I/PP1 complex regulates cell morphology.
Oliver CJ, Terry-Lorenzo RT, Elliott E, Bloomer WA, Li S, Brautigan DL, Colbran RJ, Shenolikar S
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
Neurabin I, a neuronal actin-binding protein, binds protein phosphatase 1 (PP1) and p70 ribosomal S6 protein kinase (p70S6K), both proteins implicated in cytoskeletal dynamics. We expressed wild-type and mutant neurabins fused to green fluorescent protein in Cos7, HEK293, and hippocampal neurons. Biochemical and cellular studies showed that an N-terminal F-actin-binding domain dictated neurabin I localization at actin cytoskeleton and promoted disassembly of stress fibers. Deletion of the C-terminal coiled-coil and sterile alpha motif domains abolished neurabin I dimerization and induced filopodium extension. Immune complex assays showed that neurabin I recruited an active PP1 via a PP1-docking sequence,(457)KIKF(460). Mutation of the PP1-binding motif or PP1 inhibition by okadaic acid and calyculin A abolished filopodia and restored stress fibers in cells expressing neurabin I. In vitro and in vivo studies suggested that the actin-binding domain attenuated protein kinase A (PKA) phosphorylation of neurabin I. Modification of a major PKA site, serine-461, impaired PP1 binding. Finally, p70S6K was excluded from neurabin I/PP1 complexes and required the displacement of PP1 for recruitment to neurabin I. These studies provided new insights into the assembly and regulation of a neurabin I/PP1 complex that controls actin rearrangement to promote spine development in mammalian neurons.
PMID : 12052877 [PubMed - Indexed for MEDLINE]
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Full Author Information
| First Name | LastName | Initials |
| Carey J | Oliver | CJ |
| Ryan T | Terry-Lorenzo | RT |
| Elizabeth | Elliott | E |
| Wendy A Christensen | Bloomer | WA |
| Shi | Li | S |
| David L | Brautigan | DL |
| Roger J | Colbran | RJ |
| Shirish | Shenolikar | S |
Affiliation: Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
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MESH categories and related page links
This article was linked to the MESH categories shown on the left below. The links on the right are related Memletics pages.
Category links from this article:- Actins - metabolism
- Animals
- Base Sequence
- Binding Sites
- Cells, Cultured
- Cytoskeleton - metabolism
- Dimerization
- Hippocampus - cytology
- Humans
- Microfilament Proteins - genetics, metabolism
- Molecular Sequence Data
- Mutation
- Nerve Tissue Proteins - genetics, metabolism
- Neurons - metabolism, ultrastructure
- Phosphoprotein Phosphatases - genetics, metabolism
- Phosphoproteins - genetics, metabolism
- Protein Phosphatase 1
- Rats
- Ribosomal Protein S6 Kinases - metabolism
- Signal Transduction
- Stress Fibers - metabolism, ultrastructure
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