A multiscale biophysical model for the recruitment of actin nucleating proteins at the membrane interface

Fatunmbi, Ololade; Bradley, Ryan; Kandy, Sreeja Kutti; Bucki, Robert; Janmey, Paul A.; Radhakrishnan, Ravi

doi:10.1039/d0sm00267d

Cited by 9 publications

(7 citation statements)

References 76 publications

(88 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gelsolin can bind to the cell membrane by PIP 2 which abrogates the gelsolin interaction with actin. Not only does the amount of phosphoinositide alter the free or actin-bound-gelsolin in cells, but also the lateral distribution of PIP 2 controls inactivation of gelsolin [49,50]. Recent studies showed that ATP competes with PIP 2 to bind with gelsolin [51,52].…”

Section: Pip 2 In Actin Dynamicsmentioning

confidence: 99%

Review of PIP2 in Cellular Signaling, Functions and Diseases

Mandal

2020

IJMS

View full text Add to dashboard Cite

Phosphoinositides play a crucial role in regulating many cellular functions, such as actin dynamics, signaling, intracellular trafficking, membrane dynamics, and cell–matrix adhesion. Central to this process is phosphatidylinositol bisphosphate (PIP2). The levels of PIP2 in the membrane are rapidly altered by the activity of phosphoinositide-directed kinases and phosphatases, and it binds to dozens of different intracellular proteins. Despite the vast literature dedicated to understanding the regulation of PIP2 in cells over past 30 years, much remains to be learned about its cellular functions. In this review, we focus on past and recent exciting results on different molecular mechanisms that regulate cellular functions by binding of specific proteins to PIP2 or by stabilizing phosphoinositide pools in different cellular compartments. Moreover, this review summarizes recent findings that implicate dysregulation of PIP2 in many diseases

show abstract

Section: Pip 2 In Actin Dynamicsmentioning

confidence: 99%

Review of PIP2 in Cellular Signaling, Functions and Diseases

Mandal

2020

IJMS

View full text Add to dashboard Cite

show abstract

“…For instance, Borau and colleagues [ 320 ] focused on the mechanosensing properties of the actomyosin network. Fatunmbi and colleagues [ 321 ] focused on the recruitment of actin nucleating proteins at the membrane interface. In contrast, Hetmanski and colleagues [ 322 ] proposed a combination of distinct modeling approaches to study rear retraction dynamics of migrating cells within 3D substrates.…”

Section: Computational Models Of Cell Migrationmentioning

confidence: 99%

Unravelling cell migration: defining movement from the cell surface

Merino-Casallo

Gómez‐Benito

Hervas-Raluy

et al. 2022

Cell Adhesion & Migration

View full text Add to dashboard Cite

Cell motility is essential for life and development. Unfortunately, cell migration is also linked to several pathological processes, such as cancer metastasis. Cells’ ability to migrate relies on many actors. Cells change their migratory strategy based on their phenotype and the properties of the surrounding microenvironment. Cell migration is, therefore, an extremely complex phenomenon. Researchers have investigated cell motility for more than a century. Recent discoveries have uncovered some of the mysteries associated with the mechanisms involved in cell migration, such as intracellular signaling and cell mechanics. These findings involve different players, including transmembrane receptors, adhesive complexes, cytoskeletal components , the nucleus, and the extracellular matrix. This review aims to give a global overview of our current understanding of cell migration.

show abstract

“…225 PIP 2 , which produces IP 3 following PLC cleavage, regulates actin-binding proteins including talin, gelsolin, ERM proteins (ezrin/radixin/moesin), formin, and actin-related protein 2/3 (ARP2/3) to mediate actin cytoskeleton dynamics. [226][227][228] A myriad of actin-binding proteins interact with PIP 2 , 229 including ERM proteins and myosin I, 230 talin, 228 formins and ARP2/3, 227 and Coronin 1A. 231 3.3.5 SOCE regulators and cytoskeletal proteins.…”

Section: [Ca 2+mentioning

confidence: 99%