Protein tyrosine phosphatases: regulatory mechanisms [PDF]
Protein‐tyrosine phosphatases are tightly controlled by various mechanisms, ranging from differential expression in specific cell types to restricted subcellular localization, limited proteolysis, post‐translational modifications affecting intrinsic catalytic activity, ligand binding and dimerization.
den Hertog, J., Ostman, A., Bohmer, F.D.
openaire +2 more sources
Interaction of kinase-interaction-motif protein tyrosine phosphatases with the mitogen-activated protein kinase ERK2. [PDF]
The mitogen-activation protein kinase ERK2 is tightly regulated by multiple phosphatases, including those of the kinase interaction motif (KIM) PTP family (STEP, PTPSL and HePTP).
Dana M Francis +4 more
doaj +1 more source
The present study offers a new approach for designing inhibitors of protein tyrosine phosphatases. We have synthesized the cyclam derivatives with α,α-difluoro-β-ketophosphonate fragments covalently attached to tetraazamacrocyclic scaffold, which is ...
D. I. Khavrienko +8 more
doaj +1 more source
A loss-of-function screen for phosphatases that regulate neurite outgrowth identifies PTPN12 as a negative regulator of TrkB tyrosine phosphorylation. [PDF]
Alterations in function of the neurotrophin BDNF are associated with neurodegeneration, cognitive decline, and psychiatric disorders. BDNF promotes axonal outgrowth and branching, regulates dendritic tree morphology and is important for axonal ...
Malene Ambjørn +8 more
doaj +1 more source
Interactions between Type III receptor tyrosine phosphatases and growth factor receptor tyrosine kinases regulate tracheal tube formation in Drosophila [PDF]
The respiratory (tracheal) system of the Drosophila melanogaster larva is an intricate branched network of air-filled tubes. Its developmental logic is similar in some ways to that of the vertebrate vascular system.
Jeon, Mili, Scott, Matthew P., Zinn, Kai
core +3 more sources
Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe +3 more
wiley +1 more source
Protein tyrosine phosphatases, together with protein tyrosine kinases, control many molecular signaling steps that control life at cellular and organismal levels. Impairing alterations in the genes encoding the involved proteins is expected to profoundly
Wiljan J. A. J. Hendriks +3 more
doaj +1 more source
A new monoclonal antibody detects downregulation of protein tyrosine phosphatase receptor type γ in chronic myeloid leukemia patients [PDF]
Background: Protein tyrosine phosphatase receptor gamma (PTPRG) is a ubiquitously expressed member of the protein tyrosine phosphatase family known to act as a tumor suppressor gene in many different neoplasms with mechanisms of inactivation including ...
Al Sayab, Ali +15 more
core +3 more sources
Tau acetylation at K331 has limited impact on tau pathology in vivo
We mapped tau post‐translational modifications in humanized MAPT knock‐in mice and in amyloid‐bearing double knock‐in mice. Acetylation within the repeat domain, particularly around K331, showed modest increases under amyloid pathology. To test functional relevance, we generated MAPTK331Q knock‐in mice.
Shoko Hashimoto +3 more
wiley +1 more source
Regulatory Functions of Protein Tyrosine Phosphatase Receptor Type O in Immune Cells
The members of the protein tyrosine phosphatase (PTP) family are key regulators in multiple signal transduction pathways and therefore they play important roles in many cellular processes, including immune response.
Feiling Xie +7 more
doaj +1 more source

