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Shu-ou Shan
California Institute of Technology
110Publications
33H-index
3,516Citations
Publications 112
Newest
#1Chien-I Yang (California Institute of Technology)
#2Hao-Hsuan Hsieh (California Institute of Technology)
Last.Shu-ou Shan (California Institute of Technology)H-Index: 33
view all 3 authors...
The nascent polypeptide exit site of the ribosome is a crowded environment where multiple ribosome-associated protein biogenesis factors (RPBs) compete for the nascent polypeptide to influence their localization, folding, or quality control. Here we address how N-terminal methionine excision (NME), a ubiquitous process crucial for the maturation of over 50% of the bacterial proteome, occurs in a timely and selective manner in this crowded environment. In bacteria, NME is mediated by 2 essential ...
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#1Yu-Hsien Hwang Fu (California Institute of Technology)H-Index: 1
#2Sowmya Chandrasekar (California Institute of Technology)H-Index: 6
Last.Shu-ou Shan (California Institute of Technology)H-Index: 33
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Molecular recognition features (MoRFs) provide interaction motifs in intrinsically disordered protein regions to mediate diverse cellular functions. Here we report that a MoRF element, located in the disordered linker domain of the mammalian signal recognition particle (SRP) receptor and conserved among eukaryotes, plays an essential role in sensing the ribosome during cotranslational protein targeting to the endoplasmic reticulum. Loss of the MoRF in the SRP receptor (SR) largely abolishes the ...
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#1Shuai Wang (California Institute of Technology)H-Index: 2
#2Ahmad Jomaa (ETH Zurich)H-Index: 11
Last.Shu-ou Shan (California Institute of Technology)H-Index: 33
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Cotranslational protein targeting is a conserved process for membrane protein biogenesis. In Escherichia coli, the essential ATPase SecA was found to cotranslationally target a subset of nascent membrane proteins to the SecYEG translocase at the plasma membrane. The molecular mechanism of this pathway remains unclear. Here we use biochemical and cryoelectron microscopy analyses to show that the amino-terminal amphipathic helix of SecA and the ribosomal protein uL23 form a composite binding site ...
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#1Shu-ou Shan (California Institute of Technology)H-Index: 33
Newly synthesized integral membrane proteins must traverse the aqueous cytosolic environment before arrival at their membrane destination and are prone to aggregation, misfolding, and mislocalization during this process. The biogenesis of integral membrane proteins therefore poses acute challenges to protein homeostasis within a cell and requires the action of effective molecular chaperones. Chaperones that mediate membrane protein targeting not only need to protect the nascent transmembrane dom...
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#1Un Seng Chio (California Institute of Technology)H-Index: 4
#2SangYoon Chung (UCLA: University of California, Los Angeles)H-Index: 10
Last.Shu-ou Shan (California Institute of Technology)H-Index: 33
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Summary Molecular chaperones play key roles in maintaining cellular proteostasis. In addition to preventing client aggregation, chaperones often relay substrates within a network while preventing off-pathway chaperones from accessing the substrate. Here we show that a conserved lid motif lining the substrate-binding groove of the Get3 ATPase enables these important functions during the targeted delivery of tail-anchored membrane proteins (TAs) to the endoplasmic reticulum. The lid prevents promi...
3 CitationsSource
#1Hyunju Cho (California Institute of Technology)H-Index: 1
#2Un Seng Chio (California Institute of Technology)H-Index: 4
Last.Shu-ou Shan (California Institute of Technology)H-Index: 33
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1 CitationsSource
#1Hyunjun Cho (California Institute of Technology)H-Index: 5
#2Shu-ou Shan (California Institute of Technology)H-Index: 33
Membrane proteins are aggregation‐prone in aqueous environments, and their biogenesis poses acute challenges to cellular protein homeostasis. How the chaperone network effectively protects integral membrane proteins during their post‐translational targeting is not well understood. Here, biochemical reconstitutions showed that the yeast cytosolic Hsp70 is responsible for capturing newly synthesized tail‐anchored membrane proteins (TAs) in the soluble form. Moreover, direct interaction of Hsp70 wi...
9 CitationsSource
#1Jae Ho Lee (California Institute of Technology)H-Index: 3
#2Sowmya Chandrasekar (California Institute of Technology)H-Index: 6
Last.Shu-ou Shan (California Institute of Technology)H-Index: 33
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Signal recognition particle (SRP) is a universally conserved targeting machine that mediates the targeted delivery of ∼30% of the proteome. The molecular mechanism by which eukaryotic SRP achieves efficient and selective protein targeting remains elusive. Here, we describe quantitative analyses of completely reconstituted human SRP (hSRP) and SRP receptor (SR). Enzymatic and fluorescence analyses showed that the ribosome, together with a functional signal sequence on the nascent polypeptide, are...
5 CitationsSource
#1Camille Z. McAvoy (California Institute of Technology)H-Index: 2
#2Alex Siegel (California Institute of Technology)H-Index: 1
Last.Shu-ou Shan (California Institute of Technology)H-Index: 33
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Integral membrane proteins are prone to aggregation and misfolding in aqueous environments and therefore require binding by molecular chaperones during their biogenesis. Chloroplast signal recognition particle 43 (cpSRP43) is an ATP-independent chaperone required for the biogenesis of the most abundant class of membrane proteins, the light-harvesting chlorophyll a/b-binding proteins (LHCPs). Previous work has shown that cpSRP43 specifically recognizes an L18 loop sequence conserved among LHCP pa...
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#1Peng Wang (Humboldt University of Berlin)H-Index: 13
#2Fu-Cheng Liang (California Institute of Technology)H-Index: 7
Last.Bernhard Grimm (Humboldt University of Berlin)H-Index: 50
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Assembly of light-harvesting complexes requires synchronization of chlorophyll (Chl) biosynthesis with biogenesis of light-harvesting Chl a/b-binding proteins (LHCPs). The chloroplast signal recognition particle (cpSRP) pathway is responsible for transport of nucleus-encoded LHCPs in the stroma of the plastid and their integration into the thylakoid membranes. Correct folding and assembly of LHCPs require the incorporation of Chls, whose biosynthesis must therefore be precisely coordinated with ...
9 CitationsSource
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