Regulation of early-endosome dynamics by phosphatidylinositol 3-phosphate binding proteins

1999 ◽  
Vol 27 (4) ◽  
pp. 662-666 ◽  
Author(s):  
M. J. Clague ◽  
A. T. Jones ◽  
I. G. Mills ◽  
D. M. Walker ◽  
S. Urbé
Keyword(s):  
Binding Proteins ◽  
Early Endosome ◽  
Phosphate Binding ◽  
Phosphatidylinositol 3

scholarly journals Enhanced resistance inTheobroma cacaoagainst oomycete and fungal pathogens by secretion of phosphatidylinositol-3-phosphate-binding proteins

2015 ◽  
Vol 14 (3) ◽  
pp. 875-886 ◽  
Author(s):  
Emily E. Helliwell ◽  
Julio Vega-Arreguín ◽  
Zi Shi ◽  
Bryan Bailey ◽  
Shunyuan Xiao ◽  
...  
Keyword(s):  
Fungal Pathogens ◽  
Binding Proteins ◽  
Phosphate Binding ◽  
Enhanced Resistance ◽  
Phosphatidylinositol 3

REGULATION OF EARLY ENDOSOME DYNAMICS BY EEA1: A PHOSPHATIDYLINOSITOL 3-PHOSPHATE BINDING PROTEIN

1999 ◽  
Vol 27 (3) ◽  
pp. A76-A76
Author(s):  
M.J. Claque ◽  
A.T. Jones ◽  
I.G. Mills ◽  
D. Walker ◽  
S. Urbé
Keyword(s):  
Binding Protein ◽  
Early Endosome ◽  
Phosphate Binding ◽  
Phosphate Binding Protein ◽  
Phosphatidylinositol 3

scholarly journals Determinants of the Endosomal Localization of Sorting Nexin 1

2005 ◽  
Vol 16 (4) ◽  
pp. 2049-2057 ◽  
Author(s):  
Qi Zhong ◽  
Martin J. Watson ◽  
Cheri S. Lazar ◽  
Andrea M. Hounslow ◽  
Jonathan P. Waltho ◽  
...  
Keyword(s):  
Binding Pocket ◽  
Early Endosome ◽  
Nmr Structure ◽  
Sorting Nexin ◽  
High Affinity ◽  
Terminal Domain ◽  
Px Domain ◽  
Phox Homology ◽  
Phosphatidylinositol 3

The sorting nexin (SNX) family of proteins is characterized by sequence-related phox homology (PX) domains. A minority of PX domains bind with high affinity to phosphatidylinositol 3-phosphate [PI(3)P], whereas the majority of PX domains exhibit low affinity that is insufficient to target them to vesicles. SNX1 is located on endosomes, but its low affinity PX domain fails to localize in vivo. The NMR structure of the PX domain of SNX1 reveals an overall fold that is similar to high-affinity PX domains. However, the phosphatidylinositol (PI) binding pocket of the SNX1 PX domain is incomplete; regions of the pocket that are well defined in high-affinity PX domains are highly mobile in SNX1. Some of this mobility is lost upon binding PI(3)P. The C-terminal domain of SNX1 is a long helical dimer that localizes to vesicles but not to the early endosome antigen-1–containing vesicles where endogenous SNX1 resides. Thus, the obligate dimerization of SNX1 that is driven by the C-terminal domain creates a high-affinity PI binding species that properly targets the holo protein to endosomes.

scholarly journals Characterization of VPS34-IN1, a selective inhibitor of Vps34, reveals that the phosphatidylinositol 3-phosphate-binding SGK3 protein kinase is a downstream target of class III phosphoinositide 3-kinase

2014 ◽  
Vol 463 (3) ◽  
pp. 413-427 ◽  
Author(s):  
Ruzica Bago ◽  
Nazma Malik ◽  
Michael J. Munson ◽  
Alan R. Prescott ◽  
Paul Davies ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Selective Inhibitor ◽  
Class Iii ◽  
Phosphate Binding ◽  
Downstream Target ◽  
Phosphoinositide 3 Kinase ◽  
Phosphatidylinositol 3

We characterize VPS34-IN, a potent and selective inhibitor of class III Vps34 PI3K. Using VPS34-IN1, we demonstrate that PtdIns(3)P, produced by Vps34 controls phosphorylation and activity of the SGK3 protein kinase.

scholarly journals Phosphate removal and recovery using immobilized phosphate binding proteins

2018 ◽  
Vol 1 ◽  
pp. 100003 ◽  
Author(s):  
Kaushik Venkiteshwaran ◽  
Nilisha Pokhrel ◽  
Faten Hussein ◽  
Edwin Antony ◽  
Brooke K. Mayer
Keyword(s):  
Binding Proteins ◽  
Phosphate Removal ◽  
Phosphate Binding ◽  
Removal And Recovery

scholarly journals Rabenosyn-5, a Novel Rab5 Effector, Is Complexed with Hvps45 and Recruited to Endosomes through a Fyve Finger Domain

2000 ◽  
Vol 151 (3) ◽  
pp. 601-612 ◽  
Author(s):  
Erik Nielsen ◽  
Savvas Christoforidis ◽  
Sandrine Uttenweiler-Joseph ◽  
Marta Miaczynska ◽  
Frederique Dewitte ◽  
...  
Keyword(s):  
Early Endosome ◽  
Effector Proteins ◽  
Endosomal Trafficking ◽  
Membrane Domains ◽  
Phosphatidylinositol 3 Kinase ◽  
Early Endosomes ◽  
Site Of Action ◽  
Endosomal Membranes ◽  
Novel Protein ◽  
Phosphatidylinositol 3

Rab5 regulates endocytic membrane traffic by specifically recruiting cytosolic effector proteins to their site of action on early endosomal membranes. We have characterized a new Rab5 effector complex involved in endosomal fusion events. This complex includes a novel protein, Rabenosyn-5, which, like the previously characterized Rab5 effector early endosome antigen 1 (EEA1), contains an FYVE finger domain and is recruited in a phosphatidylinositol-3-kinase–dependent fashion to early endosomes. Rabenosyn-5 is complexed to the Sec1-like protein hVPS45. hVPS45 does not interact directly with Rab5, therefore Rabenosyn-5 serves as a molecular link between hVPS45 and the Rab5 GTPase. This property suggests that Rabenosyn-5 is a closer mammalian functional homologue of yeast Vac1p than EEA1. Furthermore, although both EEA1 and Rabenosyn-5 are required for early endosomal fusion, only overexpression of Rabenosyn-5 inhibits cathepsin D processing, suggesting that the two proteins play distinct roles in endosomal trafficking. We propose that Rab5-dependent formation of membrane domains enriched in phosphatidylinositol-3-phosphate has evolved as a mechanism for the recruitment of multiple effector proteins to mammalian early endosomes, and that these domains are multifunctional, depending on the differing activities of the effector proteins recruited.

Sign in / Sign up

Export Citation Format

Share Document