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Literature summary for 5.2.1.8 extracted from

  • Shim, S.; Yuan, J.P.; Kim, J.Y.; Zeng, W.; Huang, G.; Milshteyn, A.; Kern, D.; Muallem, S.; Ming, G.L.; Worley, P.F.
    Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening (2009), Neuron, 64, 471-483.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.2.1.8

Protein Variants

Protein Variants Comment Organism
additional information overexpression of mutant FKBP52-FD67DV, but not of wild-type FKBP52, leads to similar midline targeting errors and premature fasciculation Xenopus laevis
additional information overexpression of mutant FKBP52-FD67DV, but not of wild-type FKBP52, leads to similar midline targeting errors and premature fasciculation Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
GPI-1046
-
 Rattus norvegicus
GPI-1046
-
 Xenopus laevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Xenopus laevis FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview ?
-
 ?
additional information Rattus norvegicus FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus O42123 FKBP12
-
Xenopus laevis Q62658 FKBP12
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-
embryo
-
 Xenopus laevis
-
hippocampus
-
 Rattus norvegicus
-
neuron
-
 Xenopus laevis
-
neuron
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview Xenopus laevis ?
-
 ?
additional information FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
FKBP12
-
 Xenopus laevis
FKBP12
-
 Rattus norvegicus
FKBP52
-
 Xenopus laevis
FKBP52
-
 Rattus norvegicus
More the enzyme is a member of the FKBP family Xenopus laevis
More the enzyme is a member of the FKBP family Rattus norvegicus
peptidyl-prolyl isomerase
-
 Xenopus laevis
peptidyl-prolyl isomerase
-
 Rattus norvegicus
PPIase
-
 Xenopus laevis
PPIase
-
 Rattus norvegicus

General Information

General Information Comment Organism
physiological function FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion Xenopus laevis
physiological function FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion Rattus norvegicus