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

Myristoylation alters retinoic acid-induced down-regulation of MARCKS in immortalized hippocampal cells.

Biochemical and biophysical research communications - 16 Sept 2000

Wang L, Watson D G, Lenox R H

Abstract excerpt

The myristoylated alanine-rich C kinase substrate (MARCKS) is a prominent PKC-substrate in the brain, which has been implicated in brain development, cytoskeletal remodeling, calcium/calmodulin signaling, and neuroplasticity. The sequence of the Macs gene codes for a protein that has three highly conserved domains including a 5' myristoylation region and a 25-amino-acid phosphorylation site domain (PSD), which...

Read the complete abstract on PubMed

Topics

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

Share to Antineoplastic Agents
Share to Cell Line, Transformed

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

Share to Down-Regulation

Share to Hippocampus

Share to Intracellular Signaling Peptides and Proteins

Share to Protein Kinase C

Share to Proteins

Share to Tretinoin

Source

Identifiers

PMID: 11006104
DOI: 10.1006/bbrc.2000.3430

Genes

MARCKS
PSD

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 · 12 closest

Myristoylation alters retinoic acid-induced down-regulation of MARCKS in immortalized hippocampal cells.PMID 11006104Read ↗

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

Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin.Semantic proximity Read ↗

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

MARCKS regulates membrane ruffling and cell spreading.Semantic proximity Read ↗

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

Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons.Semantic proximity Read ↗

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

Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway.Semantic proximity Read ↗

Activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation.Semantic proximity Read ↗

Deletion of the regulatory domain of protein kinase C alpha exposes regions in the hinge and catalytic domains that mediate nuclear targeting.Semantic proximity Read ↗

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