Strategies for Site‐Specific Labeling of Receptor Proteins on the Surfaces of Living Cells by Using Genetically Encoded Peptide Tags

Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site‐specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportuni...

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Published inChembiochem : a European journal of chemical biology Vol. 22; no. 10; pp. 1717 - 1732
Main Authors Wolf, Philipp, Gavins, Georgina, Beck‐Sickinger, Annette G., Seitz, Oliver
Format Journal Article
LanguageEnglish
Published Germany Wiley Subscription Services, Inc 14.05.2021
John Wiley and Sons Inc
Subjects
Animals
bioorganic chemistry
Cell surface
Cellular communication
Coils
Complementation
Coordination compounds
Fluorescence
Fluorescence microscopy
Fluorescence Resonance Energy Transfer
Fluorescent Dyes - chemistry
Genetic code
Humans
Kinases
Labeling
Luminescent Proteins - chemistry
Luminescent Proteins - metabolism
membrane proteins
Metal complexes
Microscopy, Fluorescence
Peptides
Peptides - chemistry
Peptides - metabolism
Perturbation
protein modification
Proteins
Receptor Protein-Tyrosine Kinases - chemistry
Receptor Protein-Tyrosine Kinases - metabolism
Receptors
Receptors, G-Protein-Coupled - chemistry
Receptors, G-Protein-Coupled - metabolism
Review
Reviews
signal transduction
Staining and Labeling - methods
Tags
Tyrosine
protein modification
membrane proteins
signal transduction
fluorescence microscopy
bioorganic chemistry
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Abstract Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site‐specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportunity to combine inducible labeling with small tag sizes that avoid receptor perturbation. Herein, we review the current state of live‐cell labeling of peptide‐tagged cell‐surface proteins. Considering their importance as targets in medicinal chemistry, we focus on membrane receptors such as G protein‐coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). We discuss peptide tags that i) are subject to enzyme‐mediated modification reactions, ii) guide the complementation of reporter proteins, iii) form coiled‐coil complexes, and iv) interact with metal complexes. Given our own contributions in the field, we place emphasis on peptide‐templated labeling chemistry. Fluorescence microscopy imaging provides information about the localization and trafficking of G protein‐coupled receptors and receptor tyrosine kinases. To visualize these proteins, reporter groups must be introduced on the surface of live cells. This review discusses live‐cell protein labelling by small, genetically encoded peptide tags serving as enzyme substrates or recognition sites for interactions with proteins, coiled‐coil peptides and metal reagents.
AbstractList Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site‐specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportunity to combine inducible labeling with small tag sizes that avoid receptor perturbation. Herein, we review the current state of live‐cell labeling of peptide‐tagged cell‐surface proteins. Considering their importance as targets in medicinal chemistry, we focus on membrane receptors such as G protein‐coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). We discuss peptide tags that i) are subject to enzyme‐mediated modification reactions, ii) guide the complementation of reporter proteins, iii) form coiled‐coil complexes, and iv) interact with metal complexes. Given our own contributions in the field, we place emphasis on peptide‐templated labeling chemistry.
Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site-specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportunity to combine inducible labeling with small tag sizes that avoid receptor perturbation. Herein, we review the current state of live-cell labeling of peptide-tagged cell-surface proteins. Considering their importance as targets in medicinal chemistry, we focus on membrane receptors such as G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). We discuss peptide tags that i) are subject to enzyme-mediated modification reactions, ii) guide the complementation of reporter proteins, iii) form coiled-coil complexes, and iv) interact with metal complexes. Given our own contributions in the field, we place emphasis on peptide-templated labeling chemistry.Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site-specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportunity to combine inducible labeling with small tag sizes that avoid receptor perturbation. Herein, we review the current state of live-cell labeling of peptide-tagged cell-surface proteins. Considering their importance as targets in medicinal chemistry, we focus on membrane receptors such as G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). We discuss peptide tags that i) are subject to enzyme-mediated modification reactions, ii) guide the complementation of reporter proteins, iii) form coiled-coil complexes, and iv) interact with metal complexes. Given our own contributions in the field, we place emphasis on peptide-templated labeling chemistry.
Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site‐specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportunity to combine inducible labeling with small tag sizes that avoid receptor perturbation. Herein, we review the current state of live‐cell labeling of peptide‐tagged cell‐surface proteins. Considering their importance as targets in medicinal chemistry, we focus on membrane receptors such as G protein‐coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). We discuss peptide tags that i) are subject to enzyme‐mediated modification reactions, ii) guide the complementation of reporter proteins, iii) form coiled‐coil complexes, and iv) interact with metal complexes. Given our own contributions in the field, we place emphasis on peptide‐templated labeling chemistry. Fluorescence microscopy imaging provides information about the localization and trafficking of G protein‐coupled receptors and receptor tyrosine kinases. To visualize these proteins, reporter groups must be introduced on the surface of live cells. This review discusses live‐cell protein labelling by small, genetically encoded peptide tags serving as enzyme substrates or recognition sites for interactions with proteins, coiled‐coil peptides and metal reagents.
Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site‐specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportunity to combine inducible labeling with small tag sizes that avoid receptor perturbation. Herein, we review the current state of live‐cell labeling of peptide‐tagged cell‐surface proteins. Considering their importance as targets in medicinal chemistry, we focus on membrane receptors such as G protein‐coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). We discuss peptide tags that i) are subject to enzyme‐mediated modification reactions, ii) guide the complementation of reporter proteins, iii) form coiled‐coil complexes, and iv) interact with metal complexes. Given our own contributions in the field, we place emphasis on peptide‐templated labeling chemistry. Fluorescence microscopy imaging provides information about the localization and trafficking of G protein‐coupled receptors and receptor tyrosine kinases. To visualize these proteins, reporter groups must be introduced on the surface of live cells. This review discusses live‐cell protein labelling by small, genetically encoded peptide tags serving as enzyme substrates or recognition sites for interactions with proteins, coiled‐coil peptides and metal reagents.
Author Seitz, Oliver
Wolf, Philipp
Gavins, Georgina
Beck‐Sickinger, Annette G.
AuthorAffiliation 1 Faculty of Life Sciences Institute of Biochemistry Leipzig University Brüderstrasse 34 04103 Leipzig Germany
2 Faculty of Mathematics and Natural Sciences Department of Chemistry Humboldt-Universität zu Berlin Brook-Taylor-Str. 2 12489 Berlin Germany
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Keywords protein modification
membrane proteins
signal transduction
fluorescence microscopy
bioorganic chemistry
Language English
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PublicationPlace_xml – name: Germany
– name: Weinheim
– name: Hoboken
PublicationTitle Chembiochem : a European journal of chemical biology
PublicationTitleAlternate Chembiochem
PublicationYear 2021
Publisher Wiley Subscription Services, Inc
John Wiley and Sons Inc
Publisher_xml – name: Wiley Subscription Services, Inc
– name: John Wiley and Sons Inc
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Snippet Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site‐specifically...
Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site-specifically...
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StartPage 1717
SubjectTerms Animals
bioorganic chemistry
Cell surface
Cellular communication
Coils
Complementation
Coordination compounds
Fluorescence
Fluorescence microscopy
Fluorescence Resonance Energy Transfer
Fluorescent Dyes - chemistry
Genetic code
Humans
Kinases
Labeling
Luminescent Proteins - chemistry
Luminescent Proteins - metabolism
membrane proteins
Metal complexes
Microscopy, Fluorescence
Peptides
Peptides - chemistry
Peptides - metabolism
Perturbation
protein modification
Proteins
Receptor Protein-Tyrosine Kinases - chemistry
Receptor Protein-Tyrosine Kinases - metabolism
Receptors
Receptors, G-Protein-Coupled - chemistry
Receptors, G-Protein-Coupled - metabolism
Review
Reviews
signal transduction
Staining and Labeling - methods
Tags
Tyrosine
Title Strategies for Site‐Specific Labeling of Receptor Proteins on the Surfaces of Living Cells by Using Genetically Encoded Peptide Tags
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fcbic.202000797
https://www.ncbi.nlm.nih.gov/pubmed/33428317
https://www.proquest.com/docview/2528847644
https://www.proquest.com/docview/2476849755
https://pubmed.ncbi.nlm.nih.gov/PMC8248378
Volume 22
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