ts for the strong correlation of LFA-1 dependent cell-cell adhesion and talin accumulation at the interface.
Another connection to F-actin is observed in the APC. DC mediated antigen presentation is an active process that requires small G-proteins of the Rac family and intact F-actin (Al-Alwan et al., 2003; Benvenuti et al., 2004). This may be in part due to the interaction if ICAM-1 with the actin cytoskeleton, in part via ERM family members.
Norcross and Paul first discussed the idea of an immunological synapse with the main “synapse-like” features being a role for Ca2+ elevation, adhesion and directed secretion and polarity (Norcross, 1984). There are a handful of studies in the 1980’s and 90’s that provide quantitative data on cytoskeletal organization, secretory apparatus polarization and Ca2+ signaling in T cell conjugates with B cells e.g. (Geiger et al., 1982; Kupfer et al., 1986; Poenie et al., 1987), in addition to above mentioned studies on adhesion. The classical picture is of cell pairs with a T cell stably appended onto the often-larger target cells like an apse on a building-which is the origin of the term synapse. In one study, a distinct annular adhesive domain and central secretory domains were resolved by electron microscopy (Schmidt et al., 1988), which foreshadows the later work by Kupfer.
The molecular organization of these interfaces was not revealed until advances in imaging in the 1990’s led to the definition of discrete localization of TCR and LFA-1 and a more specific definition of immunological synapse was proposed (Dustin et al., 1998). Springer proposed in 1990 that LFA-1 and TCR would be segregated in adhesive interfaces because they are different sizes and it would be impossible for TCR to reach the MHC in a adhesive interface mediated by LFA-1 and it would be similarly difficult for LFA-1 to squeeze into an interface defined by the smaller CD2-CD58 adhesion system, which would in turn be ideal for the TCR (Springer, 1990). Springer further proposed that exclusion of large phosphat