Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization

Feng, Miao; Gu, Changzhi; Ma, Shikui; Wang, Ying; Liu, Huijuan; Han, Ruifang; Gao, Junfei; Yi, Long; Mi, Huaifeng

doi:10.1016/j.bbrc.2011.04.050

Cited by 10 publications

(5 citation statements)

References 12 publications

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“…Further studies are required to understand this phenomenon. FKBPs generally show PPIase activity to proline-containing model peptides as PPIases (35,(65)(66). FKBP22 acts as PPIase for the folding of type III collagen but did not catalyze small peptides (Fig.…”

Section: Discussionmentioning

confidence: 99%

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

Ishikawa

Bächinger

2014

Journal of Biological Chemistry

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Background: Procollagen biosynthesis requires a large number of foldases, chaperones, and modifying enzymes. Results: FKBP22 is a foldase and chaperone that interacts with a subset of collagens. Conclusion: Collagen type-specific chaperones and foldases exist in the rER. Significance: The lack of collagen type-specific rER proteins can lead to broader or overlapping phenotypes of connective tissue disorders.

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Section: Discussionmentioning

confidence: 99%

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

Ishikawa

Bächinger

2014

Journal of Biological Chemistry

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“…FKBP23 regulates BiP ATPase activity through conformational changes of its ATPase domain (Feng et al . ). However, no work has been done to show if FKBP23 regulates tau or Aβ pathology.…”

Section: Other Fkbpsmentioning

confidence: 97%

The emerging role of peptidyl‐prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease

Blair

Baker

Sabbagh

et al. 2015

Journal of Neurochemistry

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Peptidyl-prolyl cis/trans isomerases (PPIases), a unique family of molecular chaperones, regulate protein folding at proline residues. These residues are abundant within intrinsically disordered proteins, like the microtubule-associated protein tau. Tau has been shown to become hyperphosphorylated and accumulate as one of the two main pathological hallmarks in Alzheimer's disease (AD), the other being amyloid beta (Aβ). PPIases, including Pin1, FK506-binding protein (FKBP) 52, FKBP51, and FKBP12, have been shown to interact with and regulate tau biology. This interaction is particularly important given the numerous proline-directed phosphorylation sites found on tau and the role phosphorylation has been found to play in pathogenesis. This regulation then affects downstream aggregation and oligomerization of tau. However, many PPIases have yet to be explored for their effects on tau biology, despite the high likelihood of interaction based on proline content. Moreover, Pin1, FKBP12, FKBP52, cyclophilin (Cyp) A, CypB, and CypD have been shown to also regulate Aβ production or the toxicity associated with Aβ pathology. Therefore, PPIases directly and indirectly regulate pathogenic protein multimerization in AD and represent a family rich in targets for modulating the accumulation and toxicity.

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“…Mouse FKBP23 also binds BiP [217]. This binding is Ca ++ -dependent, can suppress the ATPase activity of BiP through the PPIase activity of FKBP23 and is mediated by catalyzing the cis/trans isomerization of Pro 117 in the ATPase domain of BiP [218]. …”

Section: Chaperone Network In the Ermentioning

confidence: 99%

Orchestration of secretory protein folding by ER chaperones

Gidalevitz

Stevens

Argon

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

121

115

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The endoplasmic reticulum is a major compartment of protein biogenesis in the cell, dedicated to production of secretory, membrane and organelle proteins. The secretome has distinct structural and post-translational characteristics, since folding in the ER occurs in an environment that is distinct in terms of its ionic composition, dynamics and requirements for quality contol. The folding machinery in the ER therefore includes chaperones and folding enzymes that introduce, monitor and react to disulfide bonds, glycans, and fluctuations of luminal calcium. We describe the major chaperone networks in the lumen and discuss how they have distinct modes of operation that enable cells to accomplish highly efficient production of the secretome.

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Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization

Cited by 10 publications

References 12 publications

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

The emerging role of peptidyl‐prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease

Orchestration of secretory protein folding by ER chaperones

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