Calcium and calmodulin-dependent serine/threonine protein kinase type II (CaMKII)-mediated intramolecular opening of integrin cytoplasmic domain-associated protein-1 (ICAP-1a) negatively regulates ß1 integrins.
AuthorsMillon-Frémillon A, Brunner M, Abed N, Collomb E, Ribba AS, Block MR, Albigès-Rizo C, Bouvard D,
Journal
PubMed ID23720740
'Focal adhesion turnover during cell migration is an integrated cyclic process requiring tight regulation of integrin function. Interaction of integrin with its ligand depends on its activation state, which is regulated by the direct recruitment of proteins onto the ß integrin chain cytoplasmic domain. We previously reported that ICAP-1a, a ... More
PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain.
'Nitric oxide (NO) biosynthesis in cerebellum is preferentially activated by calcium influx through N-methyl-D-aspartate (NMDA)-type glutamate receptors, suggesting that there is a specific link between these receptors and neuronal NO synthase (nNOS). Here, we find that PSD-95 assembles a postsynaptic protein complex containing nNOS and NMDA receptors. Formation of this ... More
Netrin-1 induces axon branching in developing cortical neurons by frequency-dependent calcium signaling pathways.
AuthorsTang F, Kalil K,
JournalJ Neurosci
PubMed ID16014732
A single axon can innervate multiple targets by collateral branching. Axon branching is thus essential for establishing CNS connectivity. However, surprisingly little is known about the mechanisms by which branching is regulated. Axons often stop elongating before branches develop and anatomical and molecular data suggest that axon branching occurs independent ... More
Calcium-calmodulin-dependent protein kinase II contributes to spinal cord central sensitization.
AuthorsFang L, Wu J, Lin Q, Willis WD,
JournalJ Neurosci
PubMed ID12019337
Calcium/calmodulin-dependent protein kinase II (CaMK II) is found throughout the CNS. It regulates calcium signaling in synaptic transmission by phosphorylating various proteins, including neuronal membrane receptors and intracellular transcription factors. Inflammation or injuries to peripheral tissues cause long-lasting increases in the responses of central nociceptive neurons to innocuous and noxious ... More