Skip To Main Content
Kyle Barrie on Muck Rack

Kyle Barrie

As seen in: Nature, Wiley Online Library, Science Magazine, BioRxiv, Mondaq
Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work. Claim your profile

Get in touch with Kyle

Contact Kyle, search articles and posts on X, monitor coverage, and track replies from one place.

Learn more about Muck Rack

Actions

Share this page

Is this you?

As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile

Articles

Mechanisms of CARMIL dimerization, autoinhibition, and capping protein binding

|
By Zhen He, Yudai Sato, Sophie R Shoemaker, Kyle Barrie, Sarah Körber, Ingrid Billault-Chaumartin, Malgorzata Boczkowska, Peter J. Carman, Omar Hamoui, Johan Peranen, Guillaume Romet-Lemonne, Antoine Jégou, Pekka Lappalainen, Roberto Dominguez Verified
| Science Magazine Verified
Abstract Capping protein (CP) regulates actin-based motility by blocking monomer exchange at the filament barbed end. Several proteins, including CARMIL, bind CP and allosterically weaken its affinity for the barbed end. CARMIL comprises pleckstrin homology (PH), leucine-rich repeat (LRR), helical dimerization (HD), CP-binding region (CBR), and proline-rich (PR) domains, but their roles in CP regulation remain unclear.
Open in Who Shared Issue with article?

Mechanism of Arp2/3 complex branch disassembly by human Coro7 - Nature Communications

|
By Malgorzata Boczkowska, Kyle Barrie, Grzegorz Rebowski, Andrew Saks, Alexis Gautreau, Nooshin Shatery Nejad, Rouba Hilal
| Nature Verified
Abstract Arp2/3 complex nucleates branched actin networks that drive cell motility and intracellular trafficking. Coronins, a family of seven proteins in humans, inhibit Arp2/3 complex in vitro and reduce branch density in cells. Coro7, a distant member of this family, features two β-propeller domains (β1β2) and C-terminal Central-Acidic (CA) domains and remains poorly studied.
Open in Who Shared Issue with article?

Structural-functional characterization of the MIRO1-TRAK1 complex - Nature Communications

|
By Erika E. Ravitch, Elana E. Baltrusaitis, Tania Pérez, Kyle Barrie, Adam Fenton
| Nature Verified
Abstract Mitochondrial Rho GTPase (MIRO) features N- and C-terminal GTPase domains (nGTPase and cGTPase) flanking two pairs of EF-hands, and functions as a master scaffold on the outer mitochondrial membrane. It regulates mitochondrial motility by recruiting trafficking kinesin-binding protein (TRAK), which in turn recruits kinesin-1 and dynein-dynactin. The MIRO-TRAK interaction remains incompletely understood.
Open in Who Shared Issue with article?
See all 15 articles