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Mammalian cells express three highly conserved inositol 1,4,5-trisphosphate (IP 3 ) receptor types (IP 3 R1, IP 3 R2 and IP 3 R3), which have broadly similar characteristics, but markedly different distributions, and form homo- or heterotetrameric Ca 2+ channels in endoplasmic reticulum (ER) membranes. A vast array of published work details how mature, ER membrane-located IP 3 receptor tetramers are regulated, but much less attention has been paid to the intriguing questions of how the tetramers are assembled and destroyed as part of their natural life cycle. Are they assembled at the ER membrane from nascent, or completely translated polypeptides? How are they disassembled and degraded? These questions and other recently defined modes of IP 3 receptor processing will be briefly reviewed.

The Making and Breaking of Inositol 1,4,5-Trisphosphate Receptor Tetramers