Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling.

Michael J Roy, Minglyanna G Surudoi, Ashleigh Kropp, Jianmei Hou, Weiwen Dai, Joshua M Hardy, Lung-Yu Liang, Thomas R Cotton, Bernhard C Lechtenberg, Toby A Dite, Xiuquan Ma, Roger J Daly, Onisha Patel, Isabelle S Lucet

June 2023 Nat Commun

Synopsis of Social media discussions

The discussions reflect a generally positive reception, highlighting the structural mapping and recognition of 14-3-3 as a molecular switch, which is seen as a key advancement. Words like 'significant,' 'reveals,' and 'potential' convey an optimistic tone, emphasizing the research's relevance and possible influence on future studies.

A
Agreement
 Moderate agreement

Most discussions acknowledge the significance of identifying 14-3-3 as a molecular switch for PEAK3 interactions, indicating general consensus with the publication's conclusions.

I
Interest
 Moderate level of interest

Posts display moderate enthusiasm, expressing curiosity about how this discovery could influence understanding of cell signaling and related fields.

E
Engagement
 Moderate level of engagement

Participants reference the structural mapping and technical aspects, showing engagement with the methodology and its implications but not deeply debating or critiquing findings.

I
Impact
 Moderate level of impact

Discussions suggest the findings could have noteworthy impact on signaling research and potential therapeutic strategies, though the tone remains cautionary and exploratory.

Social Mentions

YouTube

1 Videos

Twitter

2 Posts

Metrics

Video Views

39

Extended Reach

137,553

Social Features

3

Timeline: Posts about article

Top Social Media Posts

Posts referencing the article

PEAK Pseudokinase Interactions Reveal 14-3-3 as a Molecular Switch in Cell Signaling

PEAK Pseudokinase Interactions Reveal 14-3-3 as a Molecular Switch in Cell Signaling

This study explores how PEAK pseudokinases, especially PEAK3, regulate cell migration and signaling by interacting with key proteins like 1433. It highlights the structural basis of these interactions and their role as molecular switches in cellular processes.

STEM RTCL TV

September 26, 2023

39 views

  • bxv_biochem
    @bxv_biochem (Twitter)

    When two is a crowd - Structural mapping of PEAK pseudokinase interactions identifies 14 3 3 as a molecular switch for PEAK3/Crk signaling. https://t.co/dxd8CjGIwo
    view full post

    September 2, 2022

  • bioRxiv
    @biorxivpreprint (Twitter)

    When two is a crowd - Structural mapping of PEAK pseudokinase interactions identifies 14 3 3 as a molecular switch for PEAK3/Crk signaling. https://t.co/AnzvmyBrtC #bioRxiv
    view full post

    September 2, 2022

Abstract Synopsis

  • The study explores how PEAK pseudokinases, particularly PEAK3, help control cell behaviors like migration and growth by interacting with key proteins such as CrkII, Grb2, and 1433.
  • It reveals that PEAK3 has a specific high-affinity motif that acts as a molecular switch to regulate interactions with these proteins, especially influencing CrkII binding and downstream signaling.
  • The research provides detailed structural insights into these interactions, showing how PEAK proteins function as dynamic scaffolds that coordinate signal transduction in processes like cell movement and cancer development.