The adhesion GPCR ADGRL2 engages Gα13 to enable epidermal differentiation

X Xue Yang F Feng He (Institute of Environmental Processes and Pollution Control, School of Environment and Ecology) V Vanessa Lopez-Pajares D Douglas F. Porter K Krassimira Garbett (Department of Pharmacology, Vanderbilt Brain Institute, Vanderbilt University) Z Zurab Siprashvili (Program in Epithelial Biology, Stanford University School of Medicine) L Luca Ducoli R Robin M. Meyers D David L. Reynolds (Program in Epithelial Biology, Stanford University School of Medicine) D Duy Lan Huong Bui (Department of Pharmacology, Vanderbilt Brain Institute, Vanderbilt University) A Audrey Hong (Program in Epithelial Biology, Stanford University School of Medicine) D Duy Thanh Nguyen (Program in Epithelial Biology, Stanford University School of Medicine) Y Yuqing Jing (Department of Genetics, Stanford University School of Medicine) S Smarajit Mondal (Program in Epithelial Biology, Stanford University School of Medicine) L Lisa Ko (Program in Epithelial Biology, Stanford University School of Medicine) S Shiying Tao (Program in Epithelial Biology, Stanford University School of Medicine) B Bharti Singal (Department of Molecular and Cellular Physiology, Stanford University School of Medicine) R Richard Sando (Department of Pharmacology, Vanderbilt Brain Institute, Vanderbilt University) G Georgios Skiniotis P Paul A. Khavari

Abstract

Homeostasis relies on signaling networks controlled by cell membrane receptors. Although G-protein-coupled receptors (GPCRs) are the largest family of transmembrane receptors, their specific roles in the epidermis are not fully understood. Dual CRISPR-Flow and single cell Perturb RNA-sequencing knockout screens of all epidermal GPCRs were thus performed, uncovering an essential requirement for adhesion GPCR ADGRL2 (latrophilin 2) in epidermal differentiation. Among potential downstream guanine nucleotide-binding G proteins, ADGRL2 selectively activated Gα13. Follow-up tissue knockouts verified that Gα13 is also required for epidermal differentiation. A cryoelectron microscopy structure in lipid nanodiscs showed that ADGRL2 engages with Gα13 at multiple interfaces, including via an interaction between ADGRL2 intracellular loop 3 and a Gα13-specific QQQ glutamine triplet sequence in its GTPase domain. In situ gene mutation of this interface sequence impaired epidermal differentiation, highlighting an essential new role for an ADGRL2-Gα13 axis in epidermal differentiation.

Article Details

Volume / Issue Vol. 122, Issue 47
Published November 25, 2025
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (20)

X

Xue Yang

F

Feng He

Institute of Environmental Processes and Pollution Control, School of Environment and Ecology

V

Vanessa Lopez-Pajares

D

Douglas F. Porter

K

Krassimira Garbett

Department of Pharmacology, Vanderbilt Brain Institute, Vanderbilt University

Z

Zurab Siprashvili

Program in Epithelial Biology, Stanford University School of Medicine

L

Luca Ducoli

R

Robin M. Meyers

D

David L. Reynolds

Program in Epithelial Biology, Stanford University School of Medicine

D

Duy Lan Huong Bui

Department of Pharmacology, Vanderbilt Brain Institute, Vanderbilt University

A

Audrey Hong

Program in Epithelial Biology, Stanford University School of Medicine

D

Duy Thanh Nguyen

Program in Epithelial Biology, Stanford University School of Medicine

Y

Yuqing Jing

Department of Genetics, Stanford University School of Medicine

S

Smarajit Mondal

Program in Epithelial Biology, Stanford University School of Medicine

L

Lisa Ko

Program in Epithelial Biology, Stanford University School of Medicine

S

Shiying Tao

Program in Epithelial Biology, Stanford University School of Medicine

B

Bharti Singal

Department of Molecular and Cellular Physiology, Stanford University School of Medicine

R

Richard Sando

Department of Pharmacology, Vanderbilt Brain Institute, Vanderbilt University

G

Georgios Skiniotis

P

Paul A. Khavari