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Author Notes:

Corresponding author at: David C. Pallas, Biochemistry Department (RRC4125), Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322. Email: dpallas@emory.edu.

We thank Anita Corbett and Jennifer Jackson for critical reading of the manuscript, and Michael Konomos for advice on graphic design.

Dr. David Pallas is entitled to royalty from the sale of products related to the research described in this paper by Millipore Inc., Santa Cruz Biotechnologies Inc., Invitrogen Corp., and Novus Biologicals Inc.

In addition, this same author serves as a consultant to Millipore.

The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

The terms of these arrangements have been reviewed and approved by Emory University in accordance with its conflict of interest policies.


Research Funding:

This work was supported by the National Cancer Institute of the National Institutes of Health under award number R01CA057327 to D.C.P.


  • Striatin
  • CCM
  • Disease

STRIPAK complexes: Structure, biological function, and involvement in human diseases


Journal Title:

International Journal of Biochemistry & Cell Biology


Volume 47


, Pages 118-148

Type of Work:

Article | Post-print: After Peer Review


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–like complexes in cellular processes of multiple organisms. These studies have identified novel STRIPAK or 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 will explore possible roles of striatin family complexes in disease, especially cerebral cavernous malformation.

Copyright information:

© 2013 Elsevier Ltd. All rights reserved.

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