Differential Loss of Prolyl Isomerase or Chaperone Activity of Ran-binding Protein 2 (Ranbp2) Unveils Distinct Physiological Roles of Its Cyclophilin Domain in Proteostasis

The immunophilins, cyclophilins, catalyze peptidyl cis-trans prolyl-isomerization (PPIase), a rate-limiting step in protein folding and a conformational switch in protein function. Cyclophilins are also chaperones. Noncatalytic mutations affecting the only cyclophilins with known but distinct physio...

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Veröffentlicht in:	The Journal of biological chemistry 2014-02, Vol.289 (8), p.4600-4625
Hauptverfasser:	Cho, Kyoung-in, Patil, Hemangi, Senda, Eugene, Wang, Jessica, Yi, Haiqing, Qiu, Sunny, Yoon, Dosuk, Yu, Minzhong, Orry, Andrew, Peachey, Neal S., Ferreira, Paulo A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aging - metabolism Animals Biocatalysis Chaperone Chaperonin Down-Regulation Enzymes Evoked Potentials, Visual GTPase-Activating Proteins - metabolism HeLa Cells Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism Histone Deacetylases - metabolism Humans Mice Molecular Chaperones - chemistry Molecular Chaperones - metabolism Mutant Proteins - chemistry Mutant Proteins - metabolism Mutation - genetics Nuclear Pore Complex Proteins - chemistry Nuclear Pore Complex Proteins - deficiency Nuclear Pore Complex Proteins - metabolism Opsins - metabolism Organ Specificity Peptidylprolyl Isomerase - chemistry Peptidylprolyl Isomerase - metabolism Proteasome Protein Folding Protein Misfolding Protein Structure, Quaternary Protein Structure, Tertiary Protein Synthesis and Degradation Protein Transport Retinal Cone Photoreceptor Cells - cytology Retinal Cone Photoreceptor Cells - metabolism Small Ubiquitin-Related Modifier Proteins - metabolism STAT Transcription Factors - metabolism Structure-Activity Relationship Ubiquitin - metabolism Ubiquitination
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