𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Phosphorylation of the G protein α-subunit, Gα2, of Dictyostelium discoideum requires a functional and activated Gα2

✍ Scribed by Robert E. Gundersen

Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
99 KB
Volume
66
Category
Article
ISSN
0730-2312

No coin nor oath required. For personal study only.

✦ Synopsis

The Ga2-subunit of Dictyostelium discoideum is essential to the initial stage of the cell's developmental life cycle. In response to the extracellular chemoattractant, cAMP, Ga2 is activated and transiently phosphorylated on serine-113 [Chen et al. (1994): J Biol Chem 269:20925-20930]. The role of Ga2 phosphorylation remains elusive; cells expressing the S113A, nonphosphorylated mutation of Ga2 appear to proceed through the developmental phase normally. To gain insight into the function of Ga2 phosphorylation, the conditions for Ga2 phosphorylation were examined using a variety of a-subunit point mutations and chimeras. Mutations that block the G protein activation cycle prior to or at the hydrolysis of GTP (Ga2-S45A, Ga2-G207A, and Ga2-Q208L) preclude Ga2 phosphorylation in vivo. Phosphorylation of the Ga2-Q208L mutation does however occur in an in vitro phosphorylation assay. It appears that Ga2 phosphorylation, shown previously in vivo to require the cAMP receptor, also requires signaling through the G2 pathway. Results from the in vitro assay suggest that the substrate for phosphorylation is the a-subunit monomer.

📜 SIMILAR VOLUMES

Aggregation of Dictyostelium discoideum
Aggregation of Dictyostelium discoideum is dependent on myristoylation and membrane localization of the G protein α-subunit, Gα2
✍ Patsy A. Root; Alison Prince; Robert E. Gundersen 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 308 KB 👁 1 views

The heterotrimeric G protein, G2, from the eukaryotic organism Dictyostelium discoideum participates in signal transduction pathways which are essential to Dictyostelium's developmental life cycle. G2 is activated by cell surface cAMP receptors and in turn is required for the activation of a host of

Effect of deletion of the major brain G-
Effect of deletion of the major brain G-protein α subunit (αo) on coordination of G-protein subunits and on adenylyl cyclase activity
✍ Ulrike Mende; Bojan Zagrovic; Allison Cohen; Ying Li; Dario Valenzuela; Mark C. 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 203 KB

Heterotrimeric G-proteins, composed of alpha and betagamma subunits, transmit signals from cell-surface receptors to cellular effectors and ion channels. Cellular responses to receptor agonists depend on not only the type and amount of G-protein subunits expressed but also the ratio of alpha and bet

(G586V) substitutions in the α1 and α2 c
(G586V) substitutions in the α1 and α2 chains of collagen I: Effect of α-chain stoichiometry on the phenotype of osteogenesis imperfecta?
✍ Allan M. Lund; Flemming Skovby; Marianne Schwartz 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 166 KB 👁 1 views

Osteogenesis imperfecta (OI) is a congenital disease of connective tissue, most often caused by single amino acid substitutions of glycine residues within the triple helical region of collagen I. Collagen I consists of two alpha 1 chains and one alpha 2 chain. Thus, a substitution in the alpha 1(I)

Sodium butyrate-mediated induction of th
Sodium butyrate-mediated induction of the glycoprotein hormone α-subunit gene: Requirement for continued protein synthesis, identification of a butyrate-responsive element, and inhibition of promoter activation by 2-deoxyglucose
✍ Michael J. Haas; Dominic E. Cosgrove; Wanfen Xiong; G. Stanley Cox 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 420 KB 👁 1 views

Production of the glycoprotein hormone ␣-subunit (GPH␣) was enhanced by sodium butyrate (Btr) in HeLa cells. Induction of the HeLa ␣-subunit gene by Btr was inhibited by the simultaneous addition of cycloheximide (CHX), indicating a requirement for continued protein synthesis. Transient expression a