scholarly journals A Novel Phosphatidylserine-binding Peptide Motif Defined by an Anti-idiotypic Monoclonal Antibody

1995 ◽  
Vol 270 (49) ◽  
pp. 29075-29078 ◽  
Author(s):  
Koji Igarashi ◽  
Mizuho Kaneda ◽  
Akiko Yamaji ◽  
Takaomi C. Saido ◽  
Ushio Kikkawa ◽  
...  
2018 ◽  
Vol 293 (24) ◽  
pp. 9412-9422 ◽  
Author(s):  
Deepesh Nagarajan ◽  
Sujeesh Sukumaran ◽  
Geeta Deka ◽  
Kiran Krishnamurthy ◽  
Hanudatta S. Atreya ◽  
...  

Langmuir ◽  
2015 ◽  
Vol 31 (2) ◽  
pp. 732-740 ◽  
Author(s):  
Hirokazu Nishida ◽  
Taira Kajisa ◽  
Yuuya Miyazawa ◽  
Yuki Tabuse ◽  
Takuya Yoda ◽  
...  

2007 ◽  
Vol 48 (12) ◽  
pp. 2189-2192 ◽  
Author(s):  
Surajit Ghosh ◽  
Sandeep Verma

2021 ◽  
Author(s):  
Idil Ulengin-Talkish ◽  
Matthew AH Parson ◽  
Meredith L Jenkins ◽  
Jagoree Roy ◽  
Alexis ZL Shih ◽  
...  

Calcineurin, the conserved protein phosphatase and target of immunosuppressants, is a critical mediator of Ca2+ signaling. To discover novel calcineurin-regulated processes we examined an understudied isoform, CNAβ1. We show that unlike canonical cytosolic calcineurin, CNAβ1 localizes to the plasma membrane and Golgi due to palmitoylation of its divergent C-terminal tail, which is reversed by the ABHD17A depalmitoylase. Palmitoylation targets CNAβ1 to a distinct set of membrane-associated interactors including the phosphatidylinositol 4-kinase (PI4KA) complex containing EFR3B, PI4KA, TTC7B and FAM126A. Hydrogen-deuterium exchange reveals multiple calcineurin-PI4KA complex contacts, including a calcineurin-binding peptide motif in the disordered tail of FAM126A, which we establish as a calcineurin substrate. Calcineurin inhibitors decrease PI4P production during Gq-coupled GPCR signaling, suggesting that calcineurin dephosphorylates and promotes PI4KA complex activity. In sum, this work discovers a new calcineurin-regulated signaling pathway highlighting the PI4KA complex as a regulatory target and revealing that dynamic palmitoylation confers unique localization, substrate specificity and regulation to CNAβ1.


eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Zijun Wang ◽  
Christopher O Barnes ◽  
Rajeev Gautam ◽  
Julio C Cetrulo Lorenzi ◽  
Christian T Mayer ◽  
...  

A small fraction of HIV-1- infected humans develop broadly neutralizing antibodies (bNAbs) against HIV-1 that protect macaques from simian immunodeficiency HIV chimeric virus (SHIV). Similarly, a small number of macaques infected with SHIVs develop broadly neutralizing serologic activity, but less is known about the nature of simian antibodies. Here, we report on a monoclonal antibody, Ab1485, isolated from a macaque infected with SHIVAD8 that developed broadly neutralizing serologic activity targeting the V3-glycan region of HIV-1 Env. Ab1485 neutralizes 38.1% of HIV-1 isolates in a 42-pseudovirus panel with a geometric mean IC50 of 0.055 µg/mLl and SHIVAD8 with an IC50 of 0.028 µg/mLl. Ab1485 binds the V3-glycan epitope in a glycan-dependent manner. A 3.5 Å cryo-electron microscopy structure of Ab1485 in complex with a native-like SOSIP Env trimer showed conserved contacts with the N332gp120 glycan and gp120 GDIR peptide motif, but in a distinct Env-binding orientation relative to human V3/N332gp120 glycan-targeting bNAbs. Intravenous infusion of Ab1485 protected macaques from a high dose challenge with SHIVAD8. We conclude that macaques can develop bNAbs against the V3-glycan patch that resemble human V3-glycan bNAbs.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Idil Ulengin-Talkish ◽  
Matthew A. H. Parson ◽  
Meredith L. Jenkins ◽  
Jagoree Roy ◽  
Alexis Z. L. Shih ◽  
...  

AbstractCalcineurin, the conserved protein phosphatase and target of immunosuppressants, is a critical mediator of Ca2+ signaling. Here, to discover calcineurin-regulated processes we examined an understudied isoform, CNAβ1. We show that unlike canonical cytosolic calcineurin, CNAβ1 localizes to the plasma membrane and Golgi due to palmitoylation of its divergent C-terminal tail, which is reversed by the ABHD17A depalmitoylase. Palmitoylation targets CNAβ1 to a distinct set of membrane-associated interactors including the phosphatidylinositol 4-kinase (PI4KA) complex containing EFR3B, PI4KA, TTC7B and FAM126A. Hydrogen-deuterium exchange reveals multiple calcineurin-PI4KA complex contacts, including a calcineurin-binding peptide motif in the disordered tail of FAM126A, which we establish as a calcineurin substrate. Calcineurin inhibitors decrease PI4P production during Gq-coupled GPCR signaling, suggesting that calcineurin dephosphorylates and promotes PI4KA complex activity. In sum, this work discovers a calcineurin-regulated signaling pathway which highlights the PI4KA complex as a regulatory target and reveals that dynamic palmitoylation confers unique localization, substrate specificity and regulation to CNAβ1.


1994 ◽  
Vol 39 (6) ◽  
Author(s):  
Juan Wen ◽  
Jun Wang ◽  
JensG. Kuipers ◽  
Feng Huang ◽  
KristinaM. Williams ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document