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Article ; Online: SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly via Docking Interaction.

Yip, Ryan Pak Hong / Kwok, Doris Ching Ying / Lai, Louis Tung Faat / Ho, Siu-Ming / Wong, Ivan Chun Kit / Chan, Chi-Ping / Lau, Wilson Chun Yu / Ngo, Jacky Chi Ki

PLoS pathogens

2024 Volume 20, Issue 2, Page(s) e1011978

Abstract: Members of the serine-arginine protein kinase (SRPK) family, SRPK1 and SRPK2, phosphorylate the hepatitis B core protein (Cp) and are crucial for pregenomic RNA encapsidation during viral nucleocapsid assembly. Among them, SRPK2 exhibits higher kinase ... ...

Abstract	Members of the serine-arginine protein kinase (SRPK) family, SRPK1 and SRPK2, phosphorylate the hepatitis B core protein (Cp) and are crucial for pregenomic RNA encapsidation during viral nucleocapsid assembly. Among them, SRPK2 exhibits higher kinase activity toward Cp. In this study, we identified Cp sites that are phosphorylated by SRPK2 and demonstrated that the kinase utilizes an SRPK-specific docking groove to interact with and regulate the phosphorylation of the C-terminal arginine rich domain of Cp. We determined that direct interaction between the docking groove of SRPK2 and unphosphorylated Cp inhibited premature viral capsid assembly in vitro, whereas the phosphorylation of the viral protein reactivated the process. Pull-down assays together with the new cryo-electron microscopy structure of the HBV capsid in complex with SRPK2 revealed that the kinases decorate the surface of the viral capsid by interacting with the C-terminal domain of Cp, underscoring the importance of the docking interaction in regulating capsid assembly and pregenome packaging. Moreover, SRPK2-knockout in HepG2 cells suppressed Cp phosphorylation, indicating that SRPK2 is an important cellular kinase for HBV life cycle.
MeSH term(s)	Phosphorylation ; Capsid/metabolism ; Hepatitis B virus/metabolism ; Cryoelectron Microscopy ; Protein Serine-Threonine Kinases/metabolism ; Capsid Proteins/metabolism ; Virus Assembly/physiology ; Arginine/metabolism
Chemical Substances	Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Capsid Proteins ; Arginine (94ZLA3W45F)
Language	English
Publishing date	2024-02-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011978
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Article ; Online: Isolation of the Plant Exocyst Complex.

Leung, King Pong / Lau, Wilson Chun Yu

Methods in molecular biology (Clifton, N.J.)

2017 Volume 1662, Page(s) 243–255

Abstract: The exocyst, conserved from yeast to plants to mammals, is a hetero-octameric complex that mediates tethering of secretory vesicles to designated sites on the plasma membrane during polarized exocytosis. Because structural studies of the intact exocyst ... ...

Abstract	The exocyst, conserved from yeast to plants to mammals, is a hetero-octameric complex that mediates tethering of secretory vesicles to designated sites on the plasma membrane during polarized exocytosis. Because structural studies of the intact exocyst complex have been greatly limited by the low yields of purified proteins, many aspects of the exocyst functions remain poorly understood. Here, we present the protocols for the isolation and purification of the recombinant and the native plant exocyst complex. Given the known diversification of the exocyst subunits in plants, our protocols will likely open the possibility of unraveling the functional significance of these subunits in the context of the fully assembled exocyst complex.
MeSH term(s)	Agrobacterium tumefaciens/genetics ; Agrobacterium tumefaciens/metabolism ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis/ultrastructure ; Cell Membrane/secretion ; Cell Membrane/ultrastructure ; Cells, Cultured ; Cryoelectron Microscopy ; Electroporation/methods ; Exocytosis ; Gene Expression ; Plant Cells/metabolism ; Plant Cells/ultrastructure ; Plant Leaves/genetics ; Plant Leaves/metabolism ; Plant Leaves/ultrastructure ; Plants, Genetically Modified ; Plasmids/chemistry ; Plasmids/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/secretion ; Protoplasts/secretion ; Protoplasts/ultrastructure ; Secretory Vesicles/secretion ; Secretory Vesicles/ultrastructure ; Transformation, Genetic ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/secretion
Chemical Substances	Protein Isoforms ; Vesicular Transport Proteins
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7262-3_22
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Article ; Online: Structural Biology and Electron Microscopy of the Autophagy Molecular Machinery.

Lai, Louis Tung Faat / Ye, Hao / Zhang, Wenxin / Jiang, Liwen / Lau, Wilson Chun Yu

Cells

2019 Volume 8, Issue 12

Abstract: Autophagy is a highly regulated bulk degradation process that plays a key role in the maintenance of cellular homeostasis. During autophagy, a double membrane-bound compartment termed the autophagosome is formed through de novo nucleation and assembly of ...

Abstract	Autophagy is a highly regulated bulk degradation process that plays a key role in the maintenance of cellular homeostasis. During autophagy, a double membrane-bound compartment termed the autophagosome is formed through de novo nucleation and assembly of membrane sources to engulf unwanted cytoplasmic components and targets them to the lysosome or vacuole for degradation. Central to this process are the autophagy-related (ATG) proteins, which play a critical role in plant fitness, immunity, and environmental stress response. Over the past few years, cryo-electron microscopy (cryo-EM) and single-particle analysis has matured into a powerful and versatile technique for the structural determination of protein complexes at high resolution and has contributed greatly to our current understanding of the molecular mechanisms underlying autophagosome biogenesis. Here we describe the plant-specific ATG proteins and summarize recent structural and mechanistic studies on the protein machinery involved in autophagy initiation with an emphasis on those by single-particle analysis.
MeSH term(s)	Autophagosomes/metabolism ; Autophagosomes/ultrastructure ; Autophagy ; Autophagy-Related Proteins/chemistry ; Autophagy-Related Proteins/metabolism ; Microscopy, Electron ; Models, Molecular ; Plant Proteins/chemistry ; Plant Proteins/metabolism ; Plants/metabolism ; Plants/ultrastructure
Chemical Substances	Autophagy-Related Proteins ; Plant Proteins
Language	English
Publishing date	2019-12-12
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells8121627
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Article ; Online: Site-Selective Lysine Acetylation of Human Immunoglobulin G for Immunoliposomes and Bispecific Antibody Complexes.

Yuan, Dingdong / Zhang, Yu / Lim, King Hoo / Leung, Stephen King Pong / Yang, Xizi / Liang, Yujie / Lau, Wilson Chun Yu / Chow, Kwan T / Xia, Jiang

Journal of the American Chemical Society

2022 Volume 144, Issue 40, Page(s) 18494–18503

Abstract: Site-selective acetylation of a single lysine residue in a protein that reaches a lysine acetyltransferase's accuracy, precision, and reliability is challenging. Here, we report a peptide-guided, proximity-driven group transfer reaction that acetylates a ...

Abstract	Site-selective acetylation of a single lysine residue in a protein that reaches a lysine acetyltransferase's accuracy, precision, and reliability is challenging. Here, we report a peptide-guided, proximity-driven group transfer reaction that acetylates a single lysine residue, Lys 248, of the fragment crystallizable region (Fc region) in the heavy chain of the human Immunoglobulin G (IgG). An Fc-interacting peptide bound with the Fc domain and positioned a phenolic ester close to Lys 248, which induced a nucleophilic reaction and resulted in the transfer of an acetyl group to Lys 248. The acetylation reaction proceeded to a decent yield under the physiological condition without the need for deglycosylation, unnatural amino acids, or catalysts. Along with acetylation, functional moieties such as azide, alkyne, fluorescent molecules, or biotin could also be site-selectively installed on Lys 248, allowing IgG's further derivatization. We then synthesized an antibody-lipid conjugate and constructed antibody-conjugated liposomes (immunoliposomes), targeting HER2-positive (HER2+) cancer cells. We also built a bispecific antibody complex (bsAbC) covalently linking an anti-HER2 antibody and an anti-CD3 antibody. The bsAbC showed
MeSH term(s)	Acetylation ; Alkynes ; Antibodies, Bispecific/chemistry ; Azides ; Biotin ; Esters ; Humans ; Immunoglobulin G/chemistry ; Lipids ; Liposomes ; Lysine ; Lysine Acetyltransferases ; Reproducibility of Results
Chemical Substances	Alkynes ; Antibodies, Bispecific ; Azides ; Esters ; Immunoglobulin G ; Lipids ; Liposomes ; Biotin (6SO6U10H04) ; Lysine Acetyltransferases (EC 2.3.1.32) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2022-09-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.2c07594
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Article ; Online: Morphological Diversity, Protein Adsorption, and Cellular Uptake of Polydopamine-Coated Gold Nanoparticles.

Sy, Kwun Hei Samuel / Ho, Lok Wai Cola / Lau, Wilson Chun Yu / Ko, Ho / Choi, Chung Hang Jonathan

Langmuir : the ACS journal of surfaces and colloids

2018 Volume 34, Issue 46, Page(s) 14033–14045

Abstract: Polydopamine (PDA)-coated nanoparticles are adhesive bionanomaterials widely utilized in intracellular applications, yet how their adhesiveness affects their colloidal stability and their interactions with serum proteins and mammalian cells remain ... ...

Abstract	Polydopamine (PDA)-coated nanoparticles are adhesive bionanomaterials widely utilized in intracellular applications, yet how their adhesiveness affects their colloidal stability and their interactions with serum proteins and mammalian cells remain unclear. In this work, we systematically investigate the combined effects of dopamine (DA) concentration and polymerization time (both reaction parameters spanning 2 orders of magnitude) on the morphological diversity of PDA-coated nanoparticles by coating PDA onto gold nanoparticle cores. Independent of the DA concentration, Au@PDA NPs remain largely aggregated upon several hours of limited polymerization; interestingly, extended polymerization for 2 days or longer yield randomly aggregated NPs, nearly monodisperse NPs, or worm-like NP chains in the ascending order of DA concentration. Upon exposure to serum proteins, the specific type of proteins adsorbed to the Au@PDA NPs strongly depends upon the DA concentration. As DA concentration increases, less albumin and more hemoglobin subunits adhere. Moreover, cellular uptake is a strong function of polymerization time. Serum-stabilized Au@PDA NPs prepared by limited polymerization enter Neuro-2a and HeLa cancer cells more abundantly than those prepared by extended polymerization. Our data underscore the importance of DA concentration and polymerization time for tuning the morphology and degree of intracellular delivery of PDA-coated nanostructures.
MeSH term(s)	Adsorption ; Biological Transport ; Dopamine/chemistry ; Gold/chemistry ; HeLa Cells ; Humans ; Indoles/chemistry ; Indoles/metabolism ; Metal Nanoparticles/chemistry ; Polymers/chemistry ; Polymers/metabolism ; Protein Corona/chemistry
Chemical Substances	Indoles ; Polymers ; Protein Corona ; polydopamine ; Gold (7440-57-5) ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2018-11-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021/acs.langmuir.8b02572
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Article ; Online: A distinct giant coat protein complex II vesicle population in Arabidopsis thaliana.

Li, Baiying / Zeng, Yonglun / Cao, Wenhan / Zhang, Wenxin / Cheng, Lixin / Yin, Haidi / Wu, Qian / Wang, Xiangfeng / Huang, Yan / Lau, Wilson Chun Yu / Yao, Zhong-Ping / Guo, Yusong / Jiang, Liwen

Nature plants

2021 Volume 7, Issue 10, Page(s) 1335–1346

Abstract: Plants live as sessile organisms with large-scale gene duplication events and subsequent paralogue divergence during evolution. Notably, plant paralogues are expressed tissue-specifically and fine-tuned by phytohormones during various developmental ... ...

Abstract	Plants live as sessile organisms with large-scale gene duplication events and subsequent paralogue divergence during evolution. Notably, plant paralogues are expressed tissue-specifically and fine-tuned by phytohormones during various developmental processes. The coat protein complex II (COPII) is a highly conserved vesiculation machinery mediating protein transport from the endoplasmic reticulum to the Golgi apparatus in eukaryotes
MeSH term(s)	Abscisic Acid/metabolism ; Abscisic Acid/pharmacology ; Arabidopsis/metabolism ; COP-Coated Vesicles/metabolism ; Endoplasmic Reticulum/metabolism
Chemical Substances	Abscisic Acid (72S9A8J5GW)
Language	English
Publishing date	2021-10-07
Publishing country	England
Document type	Letter
ISSN	2055-0278
ISSN (online)	2055-0278
DOI	10.1038/s41477-021-00997-9
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Article ; Online: Structural basis of substrate recognition and thermal protection by a small heat shock protein.

Yu, Chuanyang / Leung, Stephen King Pong / Zhang, Wenxin / Lai, Louis Tung Faat / Chan, Ying Ki / Wong, Man Chit / Benlekbir, Samir / Cui, Yong / Jiang, Liwen / Lau, Wilson Chun Yu

Nature communications

2021 Volume 12, Issue 1, Page(s) 3007

Abstract: Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp-substrate complexes has been hampered by the transient and ... ...

Abstract	Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp-substrate complexes has been hampered by the transient and heterogeneous nature of their interactions, and the precise mechanisms underlying substrate recognition, promiscuity, and chaperone activity of sHsps remain unclear. Here we show the formation of a stable complex between Arabidopsis thaliana plastid sHsp, Hsp21, and its natural substrate 1-deoxy-D-xylulose 5-phosphate synthase (DXPS) under heat stress, and report cryo-electron microscopy structures of Hsp21, DXPS and Hsp21-DXPS complex at near-atomic resolution. Monomeric Hsp21 binds across the dimer interface of DXPS and engages in multivalent interactions by recognizing highly dynamic structural elements in DXPS. Hsp21 partly unfolds its central α-crystallin domain to facilitate binding of DXPS, which preserves a native-like structure. This mode of interaction suggests a mechanism of sHsps anti-aggregation activity towards a broad range of substrates.
MeSH term(s)	Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Cryoelectron Microscopy ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Heat-Shock Proteins, Small/chemistry ; Heat-Shock Proteins, Small/genetics ; Heat-Shock Proteins, Small/metabolism ; Heat-Shock Response ; Models, Molecular ; Protein Folding ; Transferases/chemistry ; Transferases/metabolism
Chemical Substances	Arabidopsis Proteins ; HSP21 protein, Arabidopsis ; Heat-Shock Proteins ; Heat-Shock Proteins, Small ; Transferases (EC 2.-) ; deoxyxylulose-5-phosphate synthase (EC 2.2.1.-)
Language	English
Publishing date	2021-05-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-23338-y
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Article ; Online: Subnanometer resolution cryo-EM structure of

Lai, Louis Tung Faat / Yu, Chuanyang / Wong, Jan Siu Kei / Lo, Ho Sing / Benlekbir, Samir / Jiang, Liwen / Lau, Wilson Chun Yu

Autophagy

2019 Volume 16, Issue 3, Page(s) 575–583

Abstract: Macroautophagy/autophagy is an essential process for the maintenance of cellular homeostasis by recycling macromolecules under normal and stress conditions. ATG9 (autophagy related 9) is the only integral membrane protein in the autophagy core machinery ... ...

Abstract	Macroautophagy/autophagy is an essential process for the maintenance of cellular homeostasis by recycling macromolecules under normal and stress conditions. ATG9 (autophagy related 9) is the only integral membrane protein in the autophagy core machinery and has a central role in mediating autophagosome formation. In cells, ATG9 exists on mobile vesicles that traffic to the growing phagophore, providing an essential membrane source for the formation of autophagosomes. Here we report the three-dimensional structure of ATG9 from
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis/ultrastructure ; Arabidopsis Proteins/metabolism ; Arabidopsis Proteins/ultrastructure ; Autophagy-Related Proteins/metabolism ; Autophagy-Related Proteins/ultrastructure ; Cryoelectron Microscopy ; Membrane Proteins/metabolism ; Membrane Proteins/ultrastructure ; Models, Molecular ; Nanotechnology ; Protein Multimerization ; Protein Structure, Secondary ; Structural Homology, Protein
Chemical Substances	APG9 protein, Arabidopsis ; Arabidopsis Proteins ; Autophagy-Related Proteins ; Membrane Proteins
Language	English
Publishing date	2019-07-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2019.1639300
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Article ; Online: The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins.

Ecroyd, Heath / Bartelt-Kirbach, Britta / Ben-Zvi, Anat / Bonavita, Raffaella / Bushman, Yevheniia / Casarotto, Elena / Cecconi, Ciro / Lau, Wilson Chun Yu / Hibshman, Jonathan D / Joosten, Joep / Kimonis, Virginia / Klevit, Rachel / Liberek, Krzysztof / McMenimen, Kathryn A / Miwa, Tsukumi / Mogk, Axel / Montepietra, Daniele / Peters, Carsten / Rocchetti, Maria Teresa /

Saman, Dominik / Sisto, Angela / Secco, Valentina / Strauch, Annika / Taguchi, Hideki / Tanguay, Morgan / Tedesco, Barbara / Toth, Melinda E / Wang, Zihao / Benesch, Justin L P / Carra, Serena

Cell stress & chaperones

2023 Volume 28, Issue 6, Page(s) 621–629

Abstract: The Fourth Cell Stress Society International workshop on small heat shock proteins (sHSPs), a follow-up to successful workshops held in 2014, 2016 and 2018, took place as a virtual meeting on the 17-18 November 2022. The meeting was designed to provide ... ...

Abstract	The Fourth Cell Stress Society International workshop on small heat shock proteins (sHSPs), a follow-up to successful workshops held in 2014, 2016 and 2018, took place as a virtual meeting on the 17-18 November 2022. The meeting was designed to provide an opportunity for those working on sHSPs to reconnect and discuss their latest work. The diversity of research in the sHSP field is reflected in the breadth of topics covered in the talks presented at this meeting. Here we summarise the presentations at this meeting and provide some perspectives on exciting future topics to be addressed in the field.
MeSH term(s)	Heat-Shock Proteins, Small/metabolism ; Proteins
Chemical Substances	Heat-Shock Proteins, Small ; Proteins
Language	English
Publishing date	2023-07-18
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	1362749-1
ISSN	1466-1268 ; 1355-8145
ISSN (online)	1466-1268
ISSN	1355-8145
DOI	10.1007/s12192-023-01360-x
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Article ; Online: Chaperonin TRiC/CCT Modulates the Folding and Activity of Leukemogenic Fusion Oncoprotein AML1-ETO.

Roh, Soung-Hun / Kasembeli, Moses / Galaz-Montoya, Jesús G / Trnka, Mike / Lau, Wilson Chun-Yu / Burlingame, Alma / Chiu, Wah / Tweardy, David J

The Journal of biological chemistry

2015 Volume 291, Issue 9, Page(s) 4732–4741

Abstract: AML1-ETO is the most common fusion oncoprotein causing acute myeloid leukemia (AML), a disease with a 5-year survival rate of only 24%. AML1-ETO functions as a rogue transcription factor, altering the expression of genes critical for myeloid cell ... ...

Abstract	AML1-ETO is the most common fusion oncoprotein causing acute myeloid leukemia (AML), a disease with a 5-year survival rate of only 24%. AML1-ETO functions as a rogue transcription factor, altering the expression of genes critical for myeloid cell development and differentiation. Currently, there are no specific therapies for AML1-ETO-positive AML. While known for decades to be the translational product of a chimeric gene created by the stable chromosome translocation t(8;21)(q22;q22), it is not known how AML1-ETO achieves its native and functional conformation or whether this process can be targeted for therapeutic benefit. Here, we show that the biosynthesis and folding of the AML1-ETO protein is facilitated by interaction with the essential eukaryotic chaperonin TRiC (or CCT). We demonstrate that a folding intermediate of AML1-ETO binds to TRiC directly, mainly through its β-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. Our results suggest that TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain, which may be targeted for therapeutic benefit.
MeSH term(s)	Animals ; Cattle ; Cell Survival ; Chaperonin Containing TCP-1/antagonists & inhibitors ; Chaperonin Containing TCP-1/chemistry ; Chaperonin Containing TCP-1/metabolism ; Core Binding Factor Alpha 2 Subunit/chemistry ; Core Binding Factor Alpha 2 Subunit/genetics ; Core Binding Factor Alpha 2 Subunit/metabolism ; Gene Expression Regulation, Neoplastic ; HEK293 Cells ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Immunoprecipitation ; Models, Molecular ; Neoplasm Proteins/antagonists & inhibitors ; Neoplasm Proteins/chemistry ; Neoplasm Proteins/metabolism ; Oncogene Proteins, Fusion/chemistry ; Oncogene Proteins, Fusion/genetics ; Oncogene Proteins, Fusion/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Conformation ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Stability ; Protein Subunits ; RUNX1 Translocation Partner 1 Protein ; Rats ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Reticulocytes/metabolism
Chemical Substances	AML1-ETO fusion protein, human ; Core Binding Factor Alpha 2 Subunit ; HSP70 Heat-Shock Proteins ; Neoplasm Proteins ; Oncogene Proteins, Fusion ; Peptide Fragments ; Protein Subunits ; RUNX1 Translocation Partner 1 Protein ; Recombinant Fusion Proteins ; TCP1 protein, human ; Chaperonin Containing TCP-1 (EC 3.6.1.-)
Language	English
Publishing date	2015-12-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M115.684878
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