Your browser doesn't support javascript.
loading
A high energy phosphate jump - From pyrophospho-inositol to pyrophospho-serine.
Ganguli, Shubhra; Shah, Akruti; Hamid, Aisha; Singh, Arpita; Palakurti, Ravichand; Bhandari, Rashna.
Afiliação
  • Ganguli S; Laboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, 500039, India; Manipal Academy of Higher Education, Manipal, 576104, India.
  • Shah A; Laboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, 500039, India; Manipal Academy of Higher Education, Manipal, 576104, India.
  • Hamid A; Laboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, 500039, India.
  • Singh A; Laboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, 500039, India.
  • Palakurti R; Laboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, 500039, India.
  • Bhandari R; Laboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, 500039, India. Electronic address: rashna@cdfd.org.in.
Adv Biol Regul ; 75: 100662, 2020 01.
Article em En | MEDLINE | ID: mdl-31668836
Inositol pyrophosphates (PP-IPs) are a class of energy rich metabolites present in all eukaryotic cells. The hydroxyl groups on these water soluble derivatives of inositol are substituted with diphosphate and monophosphate moieties. Since the discovery of PP-IPs in the early 1990s, enormous progress has been made in uncovering pleiotropic roles for these small molecules in cellular physiology. PP-IPs exert their effect on proteins in two ways - allosteric regulation by direct binding, or post-translational regulation by serine pyrophosphorylation, a modification unique to PP-IPs. Serine pyrophosphorylation is achieved by Mg2+-dependent, but enzyme independent transfer of a ß-phosphate from a PP-IP to a pre-phosphorylated serine residue located in an acidic motif, within an intrinsically disordered protein sequence. This distinctive post-translational modification has been shown to regulate diverse cellular processes, including rRNA synthesis, glycolysis, and vesicle transport. However, our understanding of the molecular details of this phosphotransfer from pyrophospho-inositol to generate pyrophospho-serine, is still nascent. This review discusses our current knowledge of protein pyrophosphorylation, and recent advances in understanding the mechanism of this important yet overlooked post-translational modification.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Serina / Transdução de Sinais / Processamento de Proteína Pós-Traducional / Difosfatos / Metabolismo Energético / Células Eucarióticas / Fosfatos de Inositol Idioma: En Revista: Adv Biol Regul Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Índia País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Serina / Transdução de Sinais / Processamento de Proteína Pós-Traducional / Difosfatos / Metabolismo Energético / Células Eucarióticas / Fosfatos de Inositol Idioma: En Revista: Adv Biol Regul Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Índia País de publicação: Reino Unido