Cav1dependent

Cav1dependent refers to cellular processes and pathways that require caveolin-1 (Cav1) for their initiation, propagation, or efficiency. Cav1 is the principal component of caveolae, small flask-shaped invaginations of the plasma membrane that are rich in cholesterol and sphingolipids. As a scaffolding protein, Cav1 organizes signaling molecules and lipid microdomains, thereby influencing endocytosis, transcytosis, and signal transduction.

Cav1-dependent processes commonly involve caveolae-mediated, clathrin-independent endocytosis. In this context, Cav1 facilitates the internalization of specific cargo, including certain toxins, lipids such as cholesterol, and select receptors. After uptake, cargo may traffic through caveosomes or be routed to distinct intracellular compartments. Cav1 also modulates signaling by organizing receptor tyrosine kinases, G-protein–coupled receptors, and kinases at the membrane, affecting pathways involving eNOS, Src family kinases, and Ras proteins.

The role of Cav1-dependent pathways is prominent in tissues with abundant caveolae, such as adipocytes, endothelial cells, and smooth muscle. Beyond endocytosis, Cav1 influences transcytosis across endothelial barriers, cholesterol homeostasis, and mechanotransduction. Regulation occurs at multiple levels, including Cav1 expression, oligomerization, and post-translational modifications like phosphorylation of Tyr14 and palmitoylation. Cav1 often cooperates with caveolin-2 for proper caveolae formation; loss or mutation of Cav1 reduces caveolae numbers and disrupts Cav1-dependent signaling and trafficking.

Pathological contexts associated with Cav1-dependent dysfunction include cancer progression, atherosclerosis, pulmonary hypertension, and metabolic disorders, where altered Cav1 expression or caveolae dynamics can modify cell signaling, endocytosis, and lipid handling.