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Literature summary for 5.2.1.8 extracted from

  • Rudrabhatla, P.; Albers, W.; Pant, H.C.
    Peptidyl-prolyl isomerase 1 regulates protein phosphatase 2A-mediated topographic phosphorylation of neurofilament proteins (2009), J. Neurosci., 29, 14869-14880.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
pharmacology Pin1 is a therapeutic target for reducing aberrant phosphorylation of NF proteins in neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of GST-tagged Pin1 Homo sapiens

Protein Variants

Protein Variants Comment Organism
A16S site-directed mutagenesis, dominant-negative Pin1 point mutation Homo sapiens
additional information silencing of Pin1 by siRNA, Pin1 siRNA-transfected neurons show the reduction in perikaryal phosphorylation of NF, siRNA inhibits okadaic acid-induced perikaryal phosphorylation of NF-M/H, immunohistochemic analysis, overview Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis Homo sapiens
additional information inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways ?
-
?
additional information Homo sapiens prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
Sprague-Dawley rats
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Homo sapiens
-
brain
-
Rattus norvegicus
-
embryo
-
Rattus norvegicus
-
neuron cortical Homo sapiens
-
neuron primary cortical, Pin1 is present in both axons and cell bodies Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways Rattus norvegicus ?
-
?
additional information prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways Homo sapiens ?
-
?
additional information Pin1 inhibits the dephosphorylation of NF by PP2A in vitro Homo sapiens ?
-
?
additional information Pin1 inhibits the dephosphorylation of NF by PP2A in vitro Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
peptidyl-prolyl isomerase 1
-
Homo sapiens
peptidyl-prolyl isomerase 1
-
Rattus norvegicus
Pin1
-
Homo sapiens
Pin1
-
Rattus norvegicus

General Information

General Information Comment Organism
physiological function Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview Rattus norvegicus
physiological function Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview Homo sapiens