Structure and function of α-crystallins: Traversing from in vitro to in vivo
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- 作者：Martin Haslbeck ; Jirka Peschek1 ; Johannes Buchner ; johannes.buchner@tum.de" class="auth_mail" title="E-mail the corresponding author ; Sevil Weinkauf ; sevil.weinkauf@tum.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：αA ; αA-crystallin ; αB ; αB-crystallin ; αL ; lens α-crystallin ; GAPDH ; glyceraldehyde-3-phosphate dehydrogenase ; sHsp ; small heat shock protein
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：1860
- 期：1
- 页码：149-166
- 全文大小：1601 K
文摘
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α-Crystallins (αA-, αB-crystallin and their mixture α-crystallin) maintain lens transparency.
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As small heat shock proteins, α-crystallins protect unfolding proteins from aggregation.
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α-Crystallins form dynamic, polydisperse homo- and hetero-oligomers of different properties.
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The structural dynamics and heterogeneity of α-crystallins are key for their chaperone function.
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The complexity of α-crystallins and current gaps between in vitro and in vivo studies are highlighted.