Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Thrombopoietin receptor is required for the oncogenic function of CALR mutants.

ABSTRACT:

SUBMITTER: Nivarthi H

PROVIDER: S-EPMC4980558 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Thrombopoietin receptor is required for the oncogenic function of CALR mutants.

Nivarthi H H Chen D D Cleary C C Kubesova B B Jäger R R Bogner E E Marty C C Pecquet C C Vainchenker W W Constantinescu S N SN Kralovics R R

Leukemia 20160217 8

PMID: 26883579

Similar Datasets

Oncogenic CALR mutant C-terminus mediates dual binding to the thrombopoietin receptor triggering complex dimerization and activation.

Project description: Not available

| S-EPMC10076285 | biostudies-literature

Oncogenic CALR Mutant C-terminus Mediates Dual Binding to the Thrombopoietin Receptor Triggering Complex Dimerization and Activation

Project description:Calreticulin (CALR) is a master lectin chaperone that guides the proper folding of integral membrane proteins in the endoplasmic reticulum. In healthy cells, CALR transiently and non-specifically interacts with thousands of immature N-glycosylated proteins through its N-terminal glycan-binding domain. Conversely, frameshift mutants of CALR turn into rogue cytokine by acquiring the ability to stably and specifically interact with the Thrombopoietin Receptor (TpoR). Strikingly, this interaction induces activation of TpoR leading to myeloproliferative neoplasms, blood cancers resulting from the overproduction of blood cells. Using a multidisciplinary approach, we unveil how the CALR frameshift mutations result in structural overhaul of the entire protein and identify the structural basis of its acquired specificty for TpoR. We further describe the mechanisms by zhich complex formation triggers TpoR dimerization and activation. In addition, we provide the first complete dynamic conformational footprints of both wild-type and mutant CALR and identify novel potentially targetable sites.

2023-04-11 | PXD034131 | Pride

Upregulation of endogenous thrombopoietin receptor (MPL) with in vivo passage of calreticulin (CALR) mutant Ba/F3 cells, highlighting MPL as the requisite cytokine receptor for CALR mediated transformation.

Project description: Not available

| S-EPMC8843802 | biostudies-literature

Mutant Calreticulin Requires Both Its Mutant C-terminus and the Thrombopoietin Receptor for Oncogenic Transformation.

Project description: Not available

| S-EPMC4851866 | biostudies-literature

Expression of CALR mutants causes mpl-dependent thrombocytosis in zebrafish.

Project description: Not available

| S-EPMC5098260 | biostudies-literature

CALR Type 1-Like Mutations Increase Endoplasmic Reticulum Free Ca<sup>2+</sup> and Induce ERK1/2 Activation Independent of Thrombopoietin Receptor Activation.

Project description: Not available