Store‐operated Ca²⁺ entry (SOCE), a mechanism regulated by the filling state of the intracellular Ca²⁺ stores, is a major pathway for Ca²⁺ influx. Hypotheses to explain the communication between the Ca²⁺ stores and plasma membrane (PM) have considered both the existence of small messenger molecules, such as a Ca²⁺‐influx factor (CIF), and both stable and de novo conformational coupling between proteins in the Ca²⁺ store and PM. Alternatively, a secretion‐like coupling model based on vesicle fusion and channel insertion in the PM has been proposed, which shares some properties with the de novo conformational coupling model, such as the role of the actin cytoskeleton and soluble N‐ethylmaleimide (NEM)‐sensitive‐factor attachment proteins receptor (SNARE) proteins. Here we review recent progress made in the characterization of the de novo conformational coupling and the secretion‐like coupling models for SOCE. We pay particular attention into the involvement of SNARE proteins and the actin cytoskeleton in both SOCE models. SNAREs are recognized as proteins involved in exocytosis, participating in vesicle transport, membrane docking, and fusion. As with secretion, a role for the cortical actin network in Ca²⁺ entry has been demonstrated in a number of cell types. In resting cells, the cytoskeleton may prevent the interaction between the Ca²⁺ stores and the PM, or preventing fusion of vesicles containing Ca²⁺ channels with the PM. These are processes in which SNARE proteins might play a crucial role upon cell activation by directing a precise interaction between the membrane of the transported organelle and the PM. © 2005 Wiley‐Liss, Inc.