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

The origin of C1A-C2 interdomain interactions in protein kinase Calpha.

The Journal of biological chemistry - 28 Oct 2005

Stahelin Robert V, Wang Jiyao, Blatner Nichole R, Rafter John D, Murray Diana, Cho Wonhwa

Abstract excerpt

The regulatory domain of protein kinase Calpha (PKCalpha) contains three membrane-targeting modules, two C1 domains (C1A and C1B) that bind diacylglycerol and phorbol ester, and the C2 domain that is responsible for the Ca2+-dependent membrane binding. Accumulating evidence suggests that C1A and C2 domains of PKCalpha are tethered in the resting state and that the tethering is released upon binding to the...

Read the complete abstract on PubMed

Topics

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

Share to Diglycerides
Share to Insecta
Share to Ions

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

Share to Phorbol Esters

Share to Phosphatidylserines

Share to Pressure

Share to Protein Kinase C-alpha

Share to Surface Plasmon Resonance

Source

Identifiers

PMID: 16079140
DOI: 10.1074/jbc.M506224200

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

The origin of C1A-C2 interdomain interactions in protein kinase Calpha.PMID 16079140Read ↗

The C2 domain of protein kinase calpha is directly involved in the diacylglycerol-dependent binding of the C1 domain to the membrane.Semantic proximity Read ↗

Differential roles of phosphatidylserine, PtdIns(4,5)P2, and PtdIns(3,4,5)P3 in plasma membrane targeting of C2 domains. Molecular dynamics simulation, membrane binding, and cell translocation studies of the PKCalpha C2 domain.Semantic proximity Read ↗

Electrostatic and hydrophobic interactions differentially tune membrane binding kinetics of the C2 domain of protein kinase Cα.Semantic proximity Read ↗

The C2 domain of PKCalpha is a Ca2+ -dependent PtdIns(4,5)P2 sensing domain: a new insight into an old pathway.Semantic proximity Read ↗

Structural Basis of Protein Kinase Cα Regulation by the C-Terminal Tail.Semantic proximity Read ↗

Specific translocation of protein kinase Calpha to the plasma membrane requires both Ca2+ and PIP2 recognition by its C2 domain.Semantic proximity Read ↗

The Role of Regulatory Domains in Maintaining Autoinhibition in the Multidomain Kinase PKCα.Semantic proximity Read ↗

Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains.Semantic proximity Read ↗

Role of the lysine-rich cluster of the C2 domain in the phosphatidylserine-dependent activation of PKCalpha.Semantic proximity Read ↗

Control of atypical PKCι membrane dissociation by tyrosine phosphorylation within a PB1-C1 interdomain interface.Semantic proximity Read ↗

Role of hydrophobic residues in the C1b domain of protein kinase C delta on ligand and phospholipid interactions.Semantic proximity Read ↗

Roles of catalytic domain residues in interfacial binding and activation of group IV cytosolic phospholipase A2.Semantic proximity Read ↗

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