Discover Community Create You

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

Neuroanatomical development in the absence of PKC phosphorylation of the myristoylated alanine-rich C-kinase substrate (MARCKS) protein.

Brain research. Developmental brain research - 12 Aug 2003

Scarlett Cameron O, Blackshear Perry J

Abstract excerpt

The myristoylated alanine-rich C-kinase substrate protein (MARCKS) is a widely expressed target of protein kinase C (PKC) phosphorylation. Disruption of Marcks in mice leads to a number of developmental defects within the central nervous system that are completely prevented by expression of an epitope-tagged wild-type human MARCKS transgene. In the present study, we investigated whether PKC phosphorylation of...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Cell-Free System

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Central Nervous System

Share to Embryonic and Fetal Development

Share to Hemagglutinins

Share to Peripheral Nerves

Share to Protein Kinase C

Share to Tongue

Source

Identifiers

PMID: 12888215
DOI: 10.1016/s0165-3806(03)00155-x

Genes

MARCKS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Neuroanatomical development in the absence of PKC phosphorylation of the myristoylated alanine-rich C-kinase substrate (MARCKS) protein.PMID 12888215Read ↗

Nonmyristoylated MARCKS complements some but not all of the developmental defects associated with MARCKS deficiency in mice.Semantic proximity Read ↗

Transgenic complementation of MARCKS deficiency with a nonmyristoylatable, pseudo-phosphorylated form of MARCKS: evidence for simultaneous positive and dominant-negative effects on central nervous system development.Semantic proximity Read ↗

Two myristoylated alanine-rich C-kinase substrate (MARCKS) paralogs are required for normal development in zebrafish.Semantic proximity Read ↗

Widespread neuronal ectopia associated with secondary defects in cerebrocortical chondroitin sulfate proteoglycans and basal lamina in MARCKS-deficient mice.Semantic proximity Read ↗

Targeted deletion of the mitogen-activated protein kinase kinase 4 gene in the nervous system causes severe brain developmental defects and premature death.Semantic proximity Read ↗

Myristoylated alanine rich C kinase substrate (MARCKS) heterozygous mutant mice exhibit deficits in hippocampal mossy fiber-CA3 long-term potentiation.Semantic proximity Read ↗

Myristoylation alters retinoic acid-induced down-regulation of MARCKS in immortalized hippocampal cells.Semantic proximity Read ↗

Developmental expression of myotonic dystrophy protein kinase in brain and its relevance to clinical phenotype.Semantic proximity Read ↗

Protein kinase Cepsilon-dependent MARCKS phosphorylation in neonatal and adult rat ventricular myocytes.Semantic proximity Read ↗

Early embryonic lethality caused by disruption of the gene for choline kinase alpha, the first enzyme in phosphatidylcholine biosynthesis.Semantic proximity Read ↗

Involvement of protein phosphatase-1-mediated MARCKS translocation in myogenic differentiation of embryonic muscle cells.Semantic proximity Read ↗

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