Phosphoinositides and inositol phosphates as molecular glues

Inositol phosphates (IPs) and phosphoinositide lipids (PIPs) are regulatory molecules critical for a wide array of functions in eukaryotic cells. Membrane PIPs have clear functions in transient recruitment of signaling proteins to membranes, and IPs have been found locked in the core of proteins as structural cofactors. However, several recent studies have suggested IPs and PIPs can mediate protein-protein interactions at the interface between proteins, functioning as natural molecular glues. Here, we present recent structural biology describing how IPs and PIPs mediate these regulatory responses at protein interfaces. In addition, we describe protein-protein interactions mediated by IPs and PIPs, for which evidence supporting a natural molecular glue role is unclear or awaits further high-resolution structural analyses. Together, we put forth that PIPs and IPs have a historically under-appreciated role at protein-protein interfaces, requiring a more systematic, structural approach to elucidate.

Authors

Institutions

Publication Details

Journal
FEBS Letters
Published
2026-06-19
DOI
https://doi.org/10.1002/1873-3468.70388
Primary Topic
Protein Kinase Regulation and GTPase Signaling
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Phosphoinositides and inositol phosphates as molecular glues

Aleshia Seaton‐Terry, Raymond D. Blind, Alexander J. Cutright, Jakub N. Kubina et al.
FEBS Letters
Protein Kinase Regulation and GTPase Signaling
article

Phosphoinositides and inositol phosphates as molecular glues

Aleshia Seaton‐Terry, Raymond D. Blind, Alexander J. Cutright, Jakub N. Kubina, Mong Na Claire Loi, Joseph W. Gilligan, Jessica Martin, Daniella Zhou, Susanna Tanada Palmu, Michael J. Arambula
article en

Abstract

Inositol phosphates (IPs) and phosphoinositide lipids (PIPs) are regulatory molecules critical for a wide array of functions in eukaryotic cells. Membrane PIPs have clear functions in transient recruitment of signaling proteins to membranes, and IPs have been found locked in the core of proteins as structural cofactors. However, several recent studies have suggested IPs and PIPs can mediate protein-protein interactions at the interface between proteins, functioning as natural molecular glues. Here, we present recent structural biology describing how IPs and PIPs mediate these regulatory responses at protein interfaces. In addition, we describe protein-protein interactions mediated by IPs and PIPs, for which evidence supporting a natural molecular glue role is unclear or awaits further high-resolution structural analyses. Together, we put forth that PIPs and IPs have a historically under-appreciated role at protein-protein interfaces, requiring a more systematic, structural approach to elucidate.

FEBS Letters
Vanderbilt University (US), Vanderbilt University Medical Center (US)
National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases
Openalex Percentile: Top 11%
Protein Kinase Regulation and GTPase Signaling
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.