FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum of<i>Neurospora crassa</i>

Tremmel, Dirk; Duarte, Margarida; Videira, Arnaldo; Tropschug, Maximilian

doi:10.1016/j.febslet.2007.04.042

Cited by 13 publications

(11 citation statements)

References 26 publications

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“…Neurospora crassa FKBP22 was reported to form a complex with BiP and other chaperones (41,67). However, this FKBP22 and the mammalian FKBP22 are structurally distinct except for the FKBP domain.…”

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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“…Presenilin-1 also binds directly to the Ryanodine receptor to modulate channel activity (Chan et al, 2000;Rybalchenko et al, 2008a), and mutant presenilin-1 increases Type 3 Ryanodine receptor levels and calcium release in mammalian cells (Chan et al, 2000). FKBP14 exhibits an EF-hand calcium-binding motif, and orthologs in yeast have been shown to form chaperone complexes in the ER (Tremmel et al, 2007). The pain gene encodes an ion channel in the transient receptor potential (TRP) family, and is involved in sensing mechanical and thermal stimuli (Tracey et al, 2003).…”

Section: Characterization Of Psn Modifiersmentioning

confidence: 98%

Identifying genes that interact with Drosophila presenilin and amyloid precursor protein

Hoef

Hughes

Livne‐Bar

et al. 2009

Genesis

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The gamma-secretase complex is involved in cleaving transmembrane proteins such as Notch and one of the genes targeted in Alzheimer's disease known as amyloid precursor protein (APP). Presenilins function within the catalytic core of gamma-secretase, and mutated forms of presenilins were identified as causative factors in familial Alzheimer's disease. Recent studies show that in addition to Notch and APP, numerous signal transduction pathways are modulated by presenilins, including intracellular calcium signaling. Thus, presenilins appear to have diverse roles. To further understand presenilin function, we searched for Presenilin-interacting genes in Drosophila by performing a genetic modifier screen for enhancers and suppressors of Presenilin-dependent Notch-related phenotypes. We identified 177 modifiers, including known members of the Notch pathway and genes involved in intracellular calcium homeostasis. We further demonstrate that 53 of these modifiers genetically interacted with APP. Characterization of these genes may provide valuable insights into Presenilin function in development and disease.

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“…Transcription of heat shock genes has been well documented in N. crassa (Britton and Kapoor 2002;Freitag et al 1997;Kapoor et al 1995;Plesofsky et al 2008;Rensing et al 1998;Tremmel et al 2007;Ungermann et al 1994) as well as in other filamentous fungi (Faircloth et al 2009;Fox et al 2007;Georg and Gomes 2007;MonteroBarrientos et al 2008;Rezaie et al 2000;Turkel et al 2006;Xavier et al 1999). However, little is known about the cell stress response to phosphate (Pi) deprivation and changes in extracellular pH.…”

Section: Introductionmentioning

confidence: 99%

Transcription of the Neurospora crassa 70-kDa class heat shock protein genes is modulated in response to extracellular pH changes

Squina

Leal

Cipriano

et al. 2010

Cell Stress and Chaperones

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Heat shock proteins belong to a conserved superfamily of molecular chaperones found in prokaryotes and eukaryotes. These proteins are linked to a myriad of physiological functions. In this study, we show that the N. crassa hsp70-1 (NCU09602.3) and hsp70-2 (NCU08693.3) genes are preferentially expressed in an acidic milieu after 15 h of cell growth in sufficient phosphate at 30°C. No significant accumulation of these transcripts was detected at alkaline pH values. Both genes accumulated to a high level in mycelia that were incubated for 1 h at 45°C, regardless of the phosphate concentration and extracellular pH changes. Transcription of the hsp70-1 and hsp70-2 genes was dependent on the pacC + background in mycelia cultured under optimal growth conditions or at 45°C. The pacC gene encodes a Zn-finger transcription factor that is involved in the regulation of gene expression by pH. Heat shock induction of these two hsp genes in mycelia incubated in low-phosphate medium was almost not altered in the nuc-1 − background under both acidic and alkaline pH conditions. The NUC-1 transcriptional regulator is involved in the derepression of nucleases, phosphatases, and transporters that are necessary for fulfilling the cell's phosphate requirements. Transcription of the hsp70-3 (NCU01499.3) gene followed a different pattern of induction-the gene was depressed under insufficient phosphate conditions but was apparently unaffected by alkalinization of the culture medium. Moreover, this gene was not induced by heat shock. These results reveal novel aspects of the heatsensing network of N. crassa.

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FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum ofNeurospora crassa

Cited by 13 publications

References 26 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

Identifying genes that interact with Drosophila presenilin and amyloid precursor protein

Transcription of the Neurospora crassa 70-kDa class heat shock protein genes is modulated in response to extracellular pH changes

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