Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of Tau and MAP2 as novel substrates of Rho-kinase and myosin phosphatase.

Journal of neurochemistry - 1 Nov 2003

Amano Mutsuki, Kaneko Takako, Maeda Akio, Nakayama Masanori, Ito Masaaki, Yamauchi Takashi, Goto Hideyuki, Fukata Yuko, Oshiro Noriko, Shinohara Azusa, Iwamatsu Akihiro, Kaibuchi Kozo

Abstract excerpt

Rho-kinase and myosin phosphatase are implicated in the phosphorylation-state of myosin light chain downstream of Rho, which is thought to induce smooth muscle contraction and stress fibre formation in non-muscle cells. Here, we found that microtubule-associated proteins, Tau and MAP2, interacted...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to CHO Cells
Share to Cricetinae
Share to Microtubule-Associated Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microtubules

Share to PC12 Cells

Share to Protein Subunits

Share to rho-Associated Kinases

Share to tau Proteins

Source

Identifiers

PMID: 14535960
DOI: 10.1046/j.1471-4159.2003.02054.x

Genes

MAP2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-14535960-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of Tau and MAP2 as novel substrates of Rho-kinase and myosin phosphatase.PMID 14535960Read ↗

Regulation of the Phosphorylation State and Microtubule-Binding Activity of Tau by Protein Phosphatase 2ASemantic proximity Read ↗

The MAP1 family of microtubule-associated proteins.Semantic proximity Read ↗

Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activitySemantic proximity Read ↗

M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells.Semantic proximity Read ↗

TRPM7 regulates myosin IIA filament stability and protein localization by heavy chain phosphorylation.Semantic proximity Read ↗

Non-muscle (NM) myosin heavy chain phosphorylation regulates the formation of NM myosin filaments, adhesome assembly and smooth muscle contraction.Semantic proximity Read ↗

Molecular characterization of microtubule-associated proteins tau and map2Semantic proximity Read ↗

Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase.Semantic proximity Read ↗

Regulated association of microtubule-associated protein 2 (MAP2) with Src and Grb2: evidence for MAP2 as a scaffolding protein.Semantic proximity Read ↗

Protein kinase network in the regulation of phosphorylation and dephosphorylation of smooth muscle myosin light chain.Semantic proximity Read ↗

Regulation of myosin light chain phosphorylation by RhoB in neuronal cells.Semantic proximity Read ↗

Phosphorylation of Thr695 and Thr850 on the myosin phosphatase target subunit: inhibitory effects and occurrence in A7r5 cells.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.