Protein phosphatase 1 is a major Ser/Thr protein phosphatase activity in eukaryotic cells. It is composed of a catalytic polypeptide (PP1C), with little substrate specificity, that interacts with a large variety of proteins of diverse structure (regulatory subunits). The diversity of holoenzymes that can be formed explain the multiplicity of cellular functions under the control of this phosphatase. In quite a few cases, regulatory subunits have an inhibitory role, downregulating the activity of the phosphatase. In this chapter we shall introduce PP1C and review the most relevant families of PP1C regulatory subunits, with particular emphasis in describing the structural basis for their interaction.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/bs.apcsb.2020.06.004 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The GPCR-like protein Smoothened (Smo) plays a pivotal role in the Hedgehog (Hh) pathway. To initiate Hh signaling, active Smo binds to and inhibits the catalytic subunit of PKA in the primary cilium, a process facilitated by G protein-coupled receptor kinase 2 (Grk2). However, the precise regulatory mechanisms underlying this process, as well as the events preceding and following Smo activation, remain poorly understood.
View Article and Find Full Text PDFDiets influence metabolism and disease susceptibility, with lysine acetyltransferases (KATs) serving as key regulators through acetyl-CoA. We have previously demonstrated that a ketogenic diet alleviates cardiac pathology, though the underlying mechanisms remain largely unknown. Here we show that KAT6A acetylation is crucial for mitochondrial function and cell growth.
View Article and Find Full Text PDFPTPA localized in the Golgi apparatus plays an important role in osteoblast differentiation.
Biochem Biophys Res Commun
January 2025
Department of Oral Morphology, Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama University, Okayama, Japan. Electronic address:
Regulatory subunits of protein phosphatase 2A (PP2A) define the substrate and functional specificity of the PP2A holoenzyme within specific organelles. While PP2A regulates osteoblast differentiation, the roles and localization of its regulatory subunits in osteoblasts remain unclear. Here, we identified PTPA, a PP2A regulatory protein, predominantly localized to the Golgi apparatus, closely overlapping with the Golgi marker Giantin.
View Article and Find Full Text PDFSusceptibility to pseudoexfoliation linked to intronic variant rs4926246 in CACNA1A: Evidence from an Indian population study.
Biochim Biophys Acta Gene Regul Mech
January 2025
School of Biological Sciences, National Institute of Science Education and Research (NISER) Bhubaneswar, P.O. Bhimpur-Padanpur, Jatni, Khurda, Odisha 752050, India; Homi Bhabha National Institute (HBNI), Training School Complex, Anushaktinagar, Mumbai 400094, India. Electronic address:
Pseudoexfoliation (PEX) is an age-related, complex systemic disorder of protein aggregopathy. It is characterized by the extracellular fibril depositions, termed PEX fibrils, initially observed in various organ tissues during pseudoexfoliation syndrome (PEXS) and with significant prominence in the eye during advanced pseudoexfoliation glaucoma (PEXG). The study explores the association between CACNA1 A (calcium channel, voltage-dependent, P/Q type, alpha 1 A subunit) variants and PEX in an Indian population.
View Article and Find Full Text PDFFunctional characterization of GAPDH2 through overexpression and dsRNA-mediated RNA interference in Synechocystis.
Int J Biol Macromol
January 2025
State Key Laboratory of Green Pesticide, International Joint Research Center for Intelligent Biosensor Technology and Health, Central China Normal University, Wuhan 430079, PR China. Electronic address:
Glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH2) plays a vital role in cell growth, stress responses, and various cellular processes in organisms. However, its functional characterization in cyanobacteria, particularly in Synechocystis sp. PCC 6803, remains largely unexplored, especially concerning its overexpression and RNA interference (RNAi) via double-stranded RNA (dsRNA).
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!