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Article ; Online: Proteins: Disorder, Folding, and Crowding.

Rhoades, Elizabeth

2019 Volume 117, Issue 1, Page(s) 3–4

MeSH term(s)	Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism
Chemical Substances	Intrinsically Disordered Proteins
Language	English
Publishing date	2019-06-20
Publishing country	United States
Document type	Editorial
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2019.06.014
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Zs.A 235: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Preface.

Rhoades, Elizabeth

Methods in enzymology

2018 Volume 611, Page(s) xix–xx

MeSH term(s)	Animals ; Fluorescence Resonance Energy Transfer ; Humans ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Mass Spectrometry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Signal Transduction
Chemical Substances	Intrinsically Disordered Proteins
Language	English
Publishing date	2018-09-25
Publishing country	United States
Document type	Editorial ; Introductory Journal Article
ISSN	1557-7988 ; 0076-6879
ISSN (online)	1557-7988
ISSN	0076-6879
DOI	10.1016/S0076-6879(18)30472-5
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Article ; Online: The C-terminus of α-Synuclein Regulates its Dynamic Cellular Internalization by Neurexin 1β.

Birol, Melissa / Muñoz, Isabella Ioana Douzoglou / Rhoades, Elizabeth

Molecular biology of the cell

2023 Volume 34, Issue 13, Page(s) br21

Abstract: The aggregation of the disordered neuronal protein, α-Synuclein (αS), is the primary pathological feature of Parkinson's disease. Current hypotheses favor cell-to-cell spread of αS species as underlying disease progression, driving interest in ... ...

Abstract	The aggregation of the disordered neuronal protein, α-Synuclein (αS), is the primary pathological feature of Parkinson's disease. Current hypotheses favor cell-to-cell spread of αS species as underlying disease progression, driving interest in identifying the molecular species and cellular processes involved in cellular internalization of αS. Prior work from our lab identified the chemically specific interaction between αS and the presynaptic adhesion protein neurexin-1β (N1β) to be capable of driving cellular internalization of both monomer and aggregated forms of αS. Here we explore the physical basis of N1β-driven internalization of αS. Specifically, we show that spontaneous internalization of αS by SH-SY5Y and HEK293 cells expressing N1β requires essentially all of the membrane-binding domain of αS; αS constructs truncated beyond residue 90 bind to N1β in the plasma membrane of HEK cells, but are not internalized. Interestingly, before internalization, αS and N1β codiffuse rapidly in the plasma membrane. αS constructs that are not internalized show very slow mobility themselves, as well as slow N1β diffusion. Finally, we find that truncated αS is capable of blocking internalization of full-length αS. Our results draw attention to the potential therapeutic value of blocking αS-N1β interactions.
MeSH term(s)	Humans ; alpha-Synuclein/chemistry ; alpha-Synuclein/metabolism ; HEK293 Cells ; Neuroblastoma ; Parkinson Disease/metabolism
Chemical Substances	alpha-Synuclein ; neurexin Ibeta (156532-80-8) ; SNCA protein, human
Language	English
Publishing date	2023-09-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E22-11-0496
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Article ; Online: The Effects of Lipids on α-Synuclein Aggregation In Vitro.

Ramirez, Jennifer / Pancoe, Samantha X / Rhoades, Elizabeth / Petersson, E James

Biomolecules

2023 Volume 13, Issue 10

Abstract: The small neuronal protein α-synuclein (αS) is found in pre-synaptic terminals and plays a role in vesicle recycling and neurotransmission. Fibrillar aggregates of αS are the hallmark of Parkinson's disease and related neurodegenerative disorders. In ... ...

Abstract	The small neuronal protein α-synuclein (αS) is found in pre-synaptic terminals and plays a role in vesicle recycling and neurotransmission. Fibrillar aggregates of αS are the hallmark of Parkinson's disease and related neurodegenerative disorders. In both health and disease, interactions with lipids influence αS's structure and function, prompting much study of the effects of lipids on αS aggregation. A comprehensive collection (126 examples) of aggregation rate data for various αS/lipid combinations was presented, including combinations of lipid variations and mutations or post-translational modifications of αS. These data were interpreted in terms of lipid structure to identify general trends. These tabulated data serve as a resource for the community to help in the interpretation of aggregation experiments with lipids and to be potentially used as inputs for computational models of lipid effects on aggregation.
MeSH term(s)	Humans ; alpha-Synuclein/metabolism ; Parkinson Disease/metabolism ; Neurodegenerative Diseases ; Lipids
Chemical Substances	alpha-Synuclein ; Lipids
Language	English
Publishing date	2023-10-02
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13101476
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Article ; Online: Single-Molecule FRET of Intrinsically Disordered Proteins.

Metskas, Lauren Ann / Rhoades, Elizabeth

Annual review of physical chemistry

2020 Volume 71, Page(s) 391–414

Abstract: Intrinsically disordered proteins (IDPs) are now widely recognized as playing critical roles in a broad range of cellular functions as well as being implicated in diverse diseases. Their lack of stable secondary structure and tertiary interactions, ... ...

Abstract	Intrinsically disordered proteins (IDPs) are now widely recognized as playing critical roles in a broad range of cellular functions as well as being implicated in diverse diseases. Their lack of stable secondary structure and tertiary interactions, coupled with their sensitivity to measurement conditions, stymies many traditional structural biology approaches. Single-molecule Förster resonance energy transfer (smFRET) is now widely used to characterize the physicochemical properties of these proteins in isolation and is being increasingly applied to more complex assemblies and experimental environments. This review provides an overview of confocal diffusion-based smFRET as an experimental tool, including descriptions of instrumentation, data analysis, and protein labeling. Recent papers are discussed that illustrate the unique capability of smFRET to provide insight into aggregation-prone IDPs, protein-protein interactions involving IDPs, and IDPs in complex experimental milieus.
MeSH term(s)	Fluorescence Resonance Energy Transfer/methods ; Humans ; Intrinsically Disordered Proteins/chemistry ; Protein Aggregates ; Single Molecule Imaging/methods
Chemical Substances	Intrinsically Disordered Proteins ; Protein Aggregates
Language	English
Publishing date	2020-02-25
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1470474-2
ISSN	1545-1593 ; 0066-426X
ISSN (online)	1545-1593
ISSN	0066-426X
DOI	10.1146/annurev-physchem-012420-104917
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Article ; Online: Measuring Interactions Between Tau and Aggregation Inducers with Single-Molecule Förster Resonance Energy Transfer.

Wickramasinghe, Sanjula P / Rhoades, Elizabeth

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

2020 Volume 2141, Page(s) 755–775

Abstract: Tau is an intrinsically disordered protein implicated in the pathogenesis of Alzheimer's disease and other neurodegenerative disorders. Here we describe the application of single-molecule Förster resonance energy transfer (smFRET) for the ... ...

Abstract	Tau is an intrinsically disordered protein implicated in the pathogenesis of Alzheimer's disease and other neurodegenerative disorders. Here we describe the application of single-molecule Förster resonance energy transfer (smFRET) for the characterization of the interactions between tau and polyphosphate, an intracellular polymer that accelerates tau aggregation. We describe the design of tau constructs, purification and fluorescent labeling of tau, and details of acquisition and analysis of smFRET data. The protocols provided here outline an approach that may be applied to the study of other intrinsically disordered proteins and their binding partners.
MeSH term(s)	Alzheimer Disease/metabolism ; Calibration ; Cell Line ; Cloning, Molecular/methods ; Cysteine/chemistry ; Fluorescence Resonance Energy Transfer/instrumentation ; Fluorescence Resonance Energy Transfer/methods ; Fluorescent Dyes ; Humans ; Intrinsically Disordered Proteins/chemistry ; Mutagenesis, Site-Directed ; Organic Chemicals ; Polyphosphates/pharmacology ; Protein Aggregates ; Protein Domains ; Recombinant Proteins/drug effects ; Recombinant Proteins/genetics ; Single Molecule Imaging/instrumentation ; Single Molecule Imaging/methods ; Spectrometry, Fluorescence/methods ; tau Proteins/drug effects ; tau Proteins/genetics
Chemical Substances	Alexa594 ; Fluorescent Dyes ; Intrinsically Disordered Proteins ; MAPT protein, human ; Organic Chemicals ; Polyphosphates ; Protein Aggregates ; Recombinant Proteins ; tau Proteins ; Cysteine (K848JZ4886)
Language	English
Publishing date	2020-07-21
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-0524-0_39
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Article ; Online: Combining non-canonical amino acid mutagenesis and native chemical ligation for multiply modifying proteins: A case study of α-synuclein post-translational modifications

Galesic, Ana / Pan, Buyan / Ramirez, Jennifer / Rhoades, Elizabeth / Pratt, Matthew R. / Petersson, E. James

Methods. 2023 Oct., v. 218 p.101-109

2023

Abstract: The Parkinson’s disease associated protein α-synuclein (αS) has been found to contain numerous post-translational modifications (PTMs), in both physiological and pathological states. One PTM site of particular interest is serine 87, which is subject to ... ...

Abstract	The Parkinson’s disease associated protein α-synuclein (αS) has been found to contain numerous post-translational modifications (PTMs), in both physiological and pathological states. One PTM site of particular interest is serine 87, which is subject to both O-linked β-N-acetylglucosamine (gS) modification and phosphorylation (pS), with αS-pS₈₇ enriched in Parkinson’s disease. An often-overlooked aspect of these PTMs is their effect on the membrane-binding properties of αS, which are important to its role in regulating neurotransmitter release. Here, we show how one can study these effects by synthesizing αS constructs containing authentic PTMs and labels for single molecule fluorescence correlation spectroscopy measurements. We synthesize αS-gS₈₇ and αS-pS₈₇ by combining native chemical ligation with genetic code expansion approaches. We introduce the fluorophore by a click reaction with a non-canonical amino acid. Beyond the specific problem of PTM effects on αS, our studies highlight the value of this combination of methods for multiply modifying proteins.
Keywords	case studies ; fluorescence correlation spectroscopy ; fluorescent dyes ; genetic code ; mutagenesis ; neurotransmitters ; phosphorylation ; serine
Language	English
Dates of publication	2023-10
Size	p. 101-109.
Publishing place	Elsevier Inc.
Document type	Article ; Online
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2023.08.002
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Article ; Online: The N-terminal disease-associated R5L Tau mutation increases microtubule shrinkage rate due to disruption of microtubule-bound Tau patches.

Cario, Alisa / Wickramasinghe, Sanjula P / Rhoades, Elizabeth / Berger, Christopher L

The Journal of biological chemistry

2022 Volume 298, Issue 11, Page(s) 102526

Abstract: Regulation of the neuronal microtubule cytoskeleton is achieved through the coordination of microtubule-associated proteins (MAPs). MAP-Tau, the most abundant MAP in the axon, functions to modulate motor motility, participate in signaling cascades, as ... ...

Abstract	Regulation of the neuronal microtubule cytoskeleton is achieved through the coordination of microtubule-associated proteins (MAPs). MAP-Tau, the most abundant MAP in the axon, functions to modulate motor motility, participate in signaling cascades, as well as directly mediate microtubule dynamics. Tau misregulation is associated with a class of neurodegenerative diseases, known as tauopathies, including progressive supranuclear palsy, Pick's disease, and Alzheimer's disease. Many disease-associated mutations in Tau are found in the C-terminal microtubule-binding domain. These mutations decrease microtubule-binding affinity and are proposed to reduce microtubule stability, leading to disease. N-terminal disease-associated mutations also exist, but the mechanistic details of their downstream effects are not as clear. Here, we investigate the effect of the progressive supranuclear palsy-associated N-terminal R5L mutation on Tau-mediated microtubule dynamics using an in vitro reconstituted system. We show that the R5L mutation does not alter Tau interactions with tubulin by fluorescence correlation spectroscopy. Using total internal reflection fluorescence microscopy, we determined that the R5L mutation has no effect on microtubule growth rate, catastrophe frequency, or rescue frequency. Rather, the R5L mutation increases microtubule shrinkage rate. We determine this is due to disruption of Tau patches, larger order Tau complexes known to form on the GDP-microtubule lattice. Altogether, these results provide insight into the role of Tau patches in mediating microtubule dynamics and suggesting a novel mechanism by which mutations in the N-terminal projection domain reduce microtubule stability.
MeSH term(s)	Humans ; Microtubules/metabolism ; Microtubules/pathology ; Mutation ; Supranuclear Palsy, Progressive/genetics ; Supranuclear Palsy, Progressive/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism ; Tauopathies/genetics ; Tauopathies/metabolism
Chemical Substances	tau Proteins
Language	English
Publishing date	2022-09-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102526
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Article ; Online: Combining non-canonical amino acid mutagenesis and native chemical ligation for multiply modifying proteins: A case study of α-synuclein post-translational modifications.

Galesic, Ana / Pan, Buyan / Ramirez, Jennifer / Rhoades, Elizabeth / Pratt, Matthew R / Petersson, E James

Methods (San Diego, Calif.)

2023 Volume 218, Page(s) 101–109

Abstract: The Parkinson's disease associated protein α-synuclein (αS) has been found to contain numerous post-translational modifications (PTMs), in both physiological and pathological states. One PTM site of particular interest is serine 87, which is subject to ... ...

Abstract	The Parkinson's disease associated protein α-synuclein (αS) has been found to contain numerous post-translational modifications (PTMs), in both physiological and pathological states. One PTM site of particular interest is serine 87, which is subject to both O-linked β-N-acetylglucosamine (gS) modification and phosphorylation (pS), with αS-pS
MeSH term(s)	Humans ; alpha-Synuclein/genetics ; alpha-Synuclein/chemistry ; alpha-Synuclein/metabolism ; Parkinson Disease/genetics ; Amino Acids/metabolism ; Protein Processing, Post-Translational ; Mutagenesis
Chemical Substances	alpha-Synuclein ; Amino Acids
Language	English
Publishing date	2023-08-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2023.08.002
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Article: Cysteine-Based Mimic of Arginylation Reproduces Neuroprotective Effects of the Authentic Post-Translational Modification on α-Synuclein

Pan, Buyan / Shimogawa, Marie / Zhao, Jun / Rhoades, Elizabeth / Kashina, Anna / Petersson, E. James

Journal of the American Chemical Society. 2022 Apr. 22, v. 144, no. 17

2022

Abstract: Arginylation is an understudied post-translational modification (PTM) involving the transfer of arginine to aspartate or glutamate sidechains in a protein. Among the targets of this PTM is α-synuclein (αS), a neuronal protein involved in regulating ... ...

Abstract	Arginylation is an understudied post-translational modification (PTM) involving the transfer of arginine to aspartate or glutamate sidechains in a protein. Among the targets of this PTM is α-synuclein (αS), a neuronal protein involved in regulating synaptic vesicles. The aggregation of αS is implicated in neurodegenerative diseases, particularly in Parkinson’s disease, and arginylation has been found to protect against this pathological process. Arginylated αS has been studied through semisynthesis involving multipart native chemical ligation (NCL), but this can be very labor-intensive with low yields. Here, we present a facile way to introduce a mimic of the arginylation modification into a protein of interest, compatible with orthogonal installation of labels such as fluorophores. We synthesize bromoacetyl arginine and react it with recombinant, site-specific cysteine mutants of αS. We validate the mimic by testing the vesicle binding affinity of mimic-arginylated αS, as well as its aggregation kinetics and monomer incorporation into fibrils, and comparing these results to those of authentically arginylated αS produced through NCL. In cultured neurons, we compare the fibril seeding capabilities of preformed fibrils carrying a small percentage of arginylated αS. We find that, consistent with authentically arginylated αS, mimic-arginylated αS does not perturb the protein’s native function but alters aggregation kinetics and monomer incorporation. Both mimic and authentically modified αS suppress aggregation in neuronal cells. Our results provide further insight into the neuroprotective effects of αS arginylation, and our alternative strategy to generate arginylated αS enables the study of this PTM in proteins not accessible through NCL.
Keywords	arginine ; aspartic acid ; cysteine ; fluorescent dyes ; glutamic acid ; neurons ; post-translational modification
Language	English
Dates of publication	2022-0422
Size	p. 7911-7918.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.2c02499
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