Actinin BioID reveals sarcomere crosstalk with oxidative metabolism through interactions with IGF2BP2

Ladha, Feria A.; Thakar, Ketan; Pettinato, Anthony M.; Legere, Nicholas; Ghahremani, Shahnaz; Cohn, Rachel; Romano, Robert; Meredith, Emily; Chen, Yu-Sheng; Hinson, J. Travis

doi:10.1016/j.celrep.2021.109512

Cited by 13 publications

(28 citation statements)

References 78 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Though this protein’s primary site of regulation is the sarcolemma of myocytes, a space that measures a mere 12 nm across, recombinant dyad proteins fused to biotin ligases did not identify significant enrichment of Rad. 42,56 On the other hand, Rad was found in a list of proteins identified by mass spectrometry after HA antibody affinity purification of heart lysates from transgenic HA-tagged junctophilin. 70 Although not compared head-to-head in the same experiments, the greater catalytic efficiency of peroxidase-based systems may lead to the detection of more rare labeling events, at the cost of identifying more bystanders as well.…”

Section: Discussionmentioning

confidence: 99%

Section: Cardiovascular Applications Of Proximity Proteomicsmentioning

confidence: 99%

“…C , Actinin interacts directly with IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2), localizing IGF2BP2 to Z disks. Data derived from Ladha et al 56…”

Section: Cardiovascular Applications Of Proximity Proteomicsmentioning

confidence: 99%

“…Using gene ontology (GO) analysis, the study also identified 99 proteins with general RNA-binding functions, such as ribosomal assembly, transcription/translation, and RNA localization and metabolism. Many of these RNA-binding proteins, 56 excluding IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2), were also identified in the Ca V 1.2-APEX list. 14 Proximity labeling methods can also be applied to elucidate subcellular RNA localization either by direct RNA labeling 57 or through proximity labeling of RNAbinding proteins followed by RNA precipitation and sequencing.…”

Section: Use Of Proximity Labeling In Cultured Ipsc-cmsmentioning

confidence: 99%

See 3 more Smart Citations

Detecting Cardiovascular Protein-Protein Interactions by Proximity Proteomics

Kushner

Liu

Eisert

et al. 2022

Circulation Research

Self Cite

View full text Add to dashboard Cite

Rapidly changing and transient protein-protein interactions regulate dynamic cellular processes in the cardiovascular system. Traditional methods, including affinity purification and mass spectrometry, have revealed many macromolecular complexes in cardiomyocytes and the vasculature. Yet these methods often fail to identify in vivo or transient protein-protein interactions. To capture these interactions in living cells and animals with subsequent mass spectrometry identification, enzyme-catalyzed proximity labeling techniques have been developed in the past decade. Although the application of this methodology to cardiovascular research is still in its infancy, the field is developing rapidly, and the promise is substantial. In this review, we outline important concepts and discuss how proximity proteomics has been applied to study physiological and pathophysiological processes relevant to the cardiovascular system.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Cardiovascular Applications Of Proximity Proteomicsmentioning

confidence: 99%

“…C , Actinin interacts directly with IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2), localizing IGF2BP2 to Z disks. Data derived from Ladha et al 56…”

Section: Cardiovascular Applications Of Proximity Proteomicsmentioning

confidence: 99%

Section: Use Of Proximity Labeling In Cultured Ipsc-cmsmentioning

confidence: 99%

See 2 more Smart Citations

Detecting Cardiovascular Protein-Protein Interactions by Proximity Proteomics

Kushner

Liu

Eisert

et al. 2022

Circulation Research

Self Cite

View full text Add to dashboard Cite

show abstract

“…Finally, while the data implicating direct 14–3-3 protein interactions with the contractile machinery are evolving, a recent publication aimed at defining alpha-actinin interacting partners at the Z-disc of the sarcomere identified both 14–3-3ε and 14–3-3γ using a proximity-dependent biotinylation (BioID) approach in hiPSC-CM [ 35 ]. To our knowledge, this represents the first study that demonstrates a 14–3-3 protein contractile protein interaction, and broadly implicates their involvement in myofibrillar assembly and/or trafficking of accessory proteins to the myofibrils.…”

Section: How 14–3-3 Interactions Combine To Modulate Ecc In Health An...mentioning

confidence: 99%

14–3-3 protein regulation of excitation–contraction coupling

Thompson

Goldspink

2021

Pflugers Arch - Eur J Physiol

View full text Add to dashboard Cite

14–3-3 proteins (14–3-3 s) are a family of highly conserved proteins that regulate many cellular processes in eukaryotes by interacting with a diverse array of client proteins. The 14–3-3 proteins have been implicated in several disease states and previous reviews have condensed the literature with respect to their structure, function, and the regulation of different cellular processes. This review focuses on the growing body of literature exploring the important role 14–3-3 proteins appear to play in regulating the biochemical and biophysical events associated with excitation–contraction coupling (ECC) in muscle. It presents both a timely and unique analysis that seeks to unite studies emphasizing the identification and diversity of 14–3-3 protein function and client protein interactions, as modulators of muscle contraction. It also highlights ideas within these two well-established but intersecting fields that support further investigation with respect to the mechanistic actions of 14–3-3 proteins in the modulation of force generation in muscle.

show abstract