Abstract
The highly conserved striatin-interacting phosphatase and kinase (STrIPAK) multimeric complex regulates the hippo signaling pathway through phosphatase activity. A recent structure of the core STrIPAK hub reveals how striatins tetramerize to serve as a scaffolding platform for the assembly of an intricate architecture, which is distinct from that of all other protein phosphatase 2A (PP2A) complexes.
MeSH terms
-
Animals
-
Calmodulin-Binding Proteins / chemistry
-
Calmodulin-Binding Proteins / metabolism
-
Calmodulin-Binding Proteins / ultrastructure
-
Cryoelectron Microscopy
-
Hippo Signaling Pathway
-
Humans
-
Membrane Proteins / chemistry
-
Membrane Proteins / metabolism
-
Membrane Proteins / ultrastructure
-
Models, Molecular
-
Multienzyme Complexes / chemistry*
-
Multienzyme Complexes / metabolism*
-
Multienzyme Complexes / ultrastructure
-
Nerve Tissue Proteins / chemistry
-
Nerve Tissue Proteins / metabolism
-
Nerve Tissue Proteins / ultrastructure
-
Protein Multimerization*
-
Protein Phosphatase 2 / chemistry*
-
Protein Phosphatase 2 / metabolism*
-
Protein Phosphatase 2 / ultrastructure
-
Protein Serine-Threonine Kinases / chemistry
-
Protein Serine-Threonine Kinases / metabolism
-
Protein Subunits / chemistry
-
Protein Subunits / metabolism
-
Signal Transduction
Substances
-
Calmodulin-Binding Proteins
-
Membrane Proteins
-
Multienzyme Complexes
-
Nerve Tissue Proteins
-
Protein Subunits
-
STRN protein, human
-
Protein Serine-Threonine Kinases
-
Protein Phosphatase 2