High impact information on Cap1

• Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells [1].
• Analysis of CAP1 knockdown cells demonstrated that this protein promotes rapid actin filament depolymerization and is important for cell morphology, migration, and endocytosis [1].
• Here, we show that CAP1 is widely expressed in mouse nonmuscle cells, whereas CAP2 is the predominant isoform in developing striated muscles [1].
• In cultured NIH3T3 and B16F1 cells, CAP1 is a highly abundant protein that colocalizes with cofilin-1 to dynamic regions of the cortical actin cytoskeleton [1].
• Finally, overexpression of Cap G in transfection assays increased the motility potential of endothelial cells [2].

Biological context of Cap1

• Three SNPs, one of which disrupts a predicted Sp1 binding site, were found in the upstream region of Cap1, a strong candidate for influencing ethanol phenotypes [3].

Anatomical context of Cap1

• We now report that a capsule-deficient (Cap-) mutant of LVS survives in the leukocytes [4].

Associations of Cap1 with chemical compounds

• After opsonization in complement component C5-deficient nonimmune serum, the Cap- mutant was ingested and survived in the leukocytes [4].

Analytical, diagnostic and therapeutic context of Cap1

• The genomic region immediately upstream of the cyclase associated protein homolog 1 (Cap1) gene was directly sequenced from PCR products [3].

References