Abstract
Three elements of the Hippo tumor suppressor pathway - MST1/2, SAV1, and RASSF1- 6 - share in common a C-terminal interaction motif termed the SARAH domain. Proteins containing this domain are capable of self-association as homodimers and also of transassociation with other SARAH domain containing proteins as well as selected additional proteins that lack this domain. Recently, the association of MST1/2 with itself or with other proteins has been shown to be regulated by phosphorylation at sites near or within the SARAH domain. In this review, we focus on recent findings regarding the regulation of such MST1/2 interactions, with an emphasis on the effects of these events on Hippo pathway activity.
| Original language | English |
|---|---|
| Pages (from-to) | 675-683 |
| Number of pages | 9 |
| Journal | Biochemical Society Transactions |
| Volume | 49 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 2021 |
Keywords
- Amino Acid Sequence
- Animals
- Binding Sites/genetics
- Cell Cycle Proteins/genetics
- Gene Expression Regulation
- Hippo Signaling Pathway/genetics
- Humans
- Intracellular Signaling Peptides and Proteins/genetics
- Multiprotein Complexes/chemistry
- Protein Domains
- Protein Multimerization
- Protein Serine-Threonine Kinases/genetics
- Sequence Homology, Amino Acid
- Serine-Threonine Kinase 3/chemistry
- Tumor Suppressor Proteins/genetics