2014
DOI: 10.1074/jbc.m114.561944
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A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

Abstract: 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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Cited by 42 publications
(68 citation statements)
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References 66 publications
(70 reference statements)
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“…The binding affinity between the SH3 domain and Hsp47 (K d = 0.26 ± 0.09 μM; Fig. 3B) is comparable to that between collagen and Hsp47 (K d = 0.2∼4 μM) (20,21). This indicates that these three molecules (i.e., collagen-Hsp47-SH3 domain) likely form an equilibrium complex at the rER exit site.…”
Section: Discussionmentioning
confidence: 68%
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“…The binding affinity between the SH3 domain and Hsp47 (K d = 0.26 ± 0.09 μM; Fig. 3B) is comparable to that between collagen and Hsp47 (K d = 0.2∼4 μM) (20,21). This indicates that these three molecules (i.e., collagen-Hsp47-SH3 domain) likely form an equilibrium complex at the rER exit site.…”
Section: Discussionmentioning
confidence: 68%
“…The SH3 domain was injected as analyte over the surface of chips, each containing one of eight different types of collagen (type I, II, III, IV, V, VI, X, or XI collagens). Hsp47 was previously shown to bind to native type I, II, III, IV, V, VI, and X collagen by this method (20,21), and was used as a positive control.…”
Section: Resultsmentioning
confidence: 99%
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