The mammalian striatin family consists of three proteins, striatin, S/G2 nuclear 
autoantigen, and zinedin. Striatin family members have no intrinsic catalytic 
activity, but rather function as scaffolding proteins. Remarkably, they organize 
multiple diverse, large signaling complexes that participate in a variety of 
cellular processes. Moreover, they appear to be regulatory/targeting subunits 
for the major eukaryotic serine/threonine protein phosphatase 2A. In addition, 
striatin family members associate with germinal center kinase III kinases as 
well as other novel components, earning these assemblies the name 
striatin-interacting phosphatase and kinase (STRIPAK) complexes. Recently, there 
has been a great increase in functional and mechanistic studies aimed at 
identifying and understanding the roles of STRIPAK and STRIPAK-like complexes in 
cellular processes of multiple organisms. These studies have identified novel 
STRIPAK and STRIPAK-like complexes and have explored their roles in specific 
signaling pathways. Together, the results of these studies have sparked 
increased interest in striatin family complexes because they have revealed roles 
in signaling, cell cycle control, apoptosis, vesicular trafficking, Golgi 
assembly, cell polarity, cell migration, neural and vascular development, and 
cardiac function. Moreover, STRIPAK complexes have been connected to clinical 
conditions, including cardiac disease, diabetes, autism, and cerebral cavernous 
malformation. In this review, we discuss the expression, localization, and 
protein domain structure of striatin family members. Then we consider the 
diverse complexes these proteins and their homologs form in various organisms, 
emphasizing what is known regarding function and regulation. Finally, we explore 
possible roles of striatin family complexes in disease, especially cerebral 
cavernous malformation.