STRIPAK complexes: structure, biological function, and involvement in human diseases.
Juyeon Hwang1, David C Pallas1
1Department of Biochemistry and Winship Cancer Institute, and Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA.
The International Journal of Biochemistry & Cell Biology
|December 17, 2013
Summary
Striatin proteins act as scaffolds, organizing signaling complexes like STRIPAK. These complexes are crucial for cellular processes and linked to diseases such as cardiac disease and cerebral cavernous malformation.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The striatin protein family comprises scaffolding proteins involved in diverse cellular signaling.
- Striatin family members regulate protein phosphatase 2A and associate with kinases, forming STRIPAK complexes.
Purpose of the Study:
- To review the expression, localization, and domain structure of striatin family members.
- To explore the diverse STRIPAK complexes and their functions across organisms.
- To investigate the role of striatin complexes in various diseases, particularly cerebral cavernous malformation.
Main Methods:
- Literature review of functional and mechanistic studies on STRIPAK complexes.
- Analysis of protein domain structure and cellular localization.
- Examination of roles in signaling pathways and disease connections.
Main Results:
- Striatin family proteins are key components of large, dynamic signaling assemblies (STRIPAK).
- STRIPAK complexes regulate fundamental cellular processes including cell cycle, migration, and development.
- STRIPAK complexes are implicated in various diseases, including cardiac conditions, diabetes, and neurological disorders.
Conclusions:
- Striatin family proteins and their associated STRIPAK complexes are vital regulators of cellular functions.
- Dysregulation of STRIPAK complexes contributes to the pathogenesis of several human diseases.
- Further research into STRIPAK complexes offers therapeutic potential for diseases like cerebral cavernous malformation.
Keywords:
8p11 myeloproliferative syndromeAJAPCARDARVCBasketBskCCMCCM patient endothelial cellsCCM-ECsCCT/TRiCCTTNBP2/NLCaMCav-1Ccm3CkaDCMDUBDiseaseDrosophila Jun N-terminal kinaseDrosophila Mob3 functional homologDrosophila Ras association domain family proteinDrosophila extracellular signal-regulated kinaseEGFREMSERMERMESERαEps15ErkFARFATFGFR1OP2GAIP-interacting protein, C terminusGAPGCKIIIGHGIPCGTPase activating proteinHBMECsHEG1HGNCHMVECsHUGO Gene Nomenclature CommitteeHUVECsHemipterousHepHippoHpoICAP-1IRF-3JraJun-related antigenK-Rev interaction trapped 1KayKrit1MASKMEKK3MLCMRMap4k4Mink1MisshapenMob3MsnMsn-like kinase 1MstMst3 and Sok1-related kinaseN-methyl-d-aspartateN-methyl-d-aspartate receptorsNDPKNLSNMDANMDARsOSMPDCD10PDGFRAPP2APPARγPTBPTPROCKRTKsRho-associated coiled coil-forming kinaseRhoAS/G(2) nuclear autoantigenSG2NASIKESINSIN-inhibitory PP2A complexSIPSLMAPSPBSRSTRIP1/2STRIPAKSok1StriatinTF-1 cell apoptosis related gene-15TFAR15TJTLR3TORC1TRAF2- and NCK-interacting kinaseTnf-αTnikToll-like receptor 3WDYsk1adenomatous polyposis coliadherens junctionarmadillo repeat domainarrhythmogenic right ventricular cardiomyopathycalmodulincaveolin-1cerebral cavernous malformation 3cerebral cavernous malformationschaperonin containing TCP-1/TCP-1 ring complexconnector of kinase to AP-1cortactin-binding protein 2/cortactin-binding protein 2, N-terminal-likedErkdJnkdMob4dRassfdeubiquitinasedilated cardiomyopathyeNOSendoplasmic reticulum–mitochondria encounter structureendothelial nitric oxide synthaseepidermal growth factor receptorepidermal growth factor receptor substrate 15estrogen receptor alphaextracellular signal-regulated kinaseezrin/radixin/moesinfactor arrestfibroblast growth factor receptor 1 oncogene partner 2focal adhesion targetinggerminal center kinase IIIglycine–histidineheart of glass 1human brain microvascular endothelial cellshuman dermal microvascular endothelial cellshuman umbilical vein endothelial cellsintegrin cytoplasmic associated protein-1interferon regulatory factor 3kayakmDiamammalian homolog of Drosophila diaphanousmammalian sterile 20-likemineralocorticoid receptormitogen-activated protein kinase kinase kinase 3mitogen-activated protein kinase kinase kinase kinase 4monopolar spindle-one-binder family 3myosin light chainnuclear localization signalnucleoside-diphosphate kinaseosmosensing scaffold for MEKK3peroxisome proliferator-activated receptor γphosphotyrosine-bindingplatelet derived growth factor receptor alphaprogrammed cell death 10protein phosphatase 2Aprotein-tyrosine phosphataseras homolog gene family member Areceptor tyrosine kinasessarcolemmal membrane-associated proteinsarcoplasmic reticulumseptation initiation networkspindle pole bodysterile 20/oxidant stress-response kinase 1striatin interacting proteins 1 and 2striatin-interacting phosphatase and kinasesuppressor of IKKɛtarget of rapamycin complex 1tight junctiontryptophan–aspartatetumor necrosis factor alphayeast Sps1/sterile-20-related kinase 1
Related Concept Videos
01:09Cytoskeletal Linker Proteins - Plakins
2.0K
Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
2.0K
02:41Protein Complex Assembly
12.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
12.5K
02:41Protein Complex Assembly
1.6K
1.6K
01:57Protein Complexes with Interchangeable Parts
2.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.1K
01:57Protein Complexes with Interchangeable Parts
1.0K
1.0K
01:56Structural Protein Function
28.9K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
28.9K