Related Experiment Video

Updated: Aug 14, 2026

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

The Molecular Structure, Expression, and Emerging Role of the 15-Leucine-Rich Repeat Containing Membrane Protein

Zi-Hao Lin1, Zhi-Chao Hu1, Chang-Qing Zhang1

  • 1Department of Orthopedic Surgery, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, 600 Yishan Road, Shanghai 200233, China.

International Journal of Molecular Sciences
|August 13, 2026
PubMed

Insights

The 15-leucine-rich repeat containing membrane protein (LRRC15) is a transmembrane protein involved in cell interactions and immune responses. Understanding LRRC15

Area of Science:

  • Biochemistry and Molecular Biology
  • Immunology
  • Cell Biology

Background:

  • The 15-leucine-rich repeat containing membrane protein (LRRC15) is a transmembrane protein belonging to the leucine-rich repeat (LRR) superfamily.
  • LRRC15 plays a role in cell-cell and cell-extracellular matrix interactions, influencing fibrogenesis, vascular invasion, tumorigenesis, and antiviral immune responses.
  • Its expression can be induced by TGF-β and IL-1β, and it has been linked to skeletal diseases like osteoporosis, osteoarthritis, and rheumatoid arthritis.

Purpose of the Study:

  • To elucidate the molecular functions and signaling pathways mediated by LRRC15.
  • To investigate the role of LRRC15 in the context of skeletal diseases and osteosarcoma.
  • To explore LRRC15 as a potential biomarker and therapeutic target for bone and joint disorders.

Main Methods:

  • Analysis of LRRC15's involvement in various cellular processes through investigation of associated signaling pathways (e.g., integrin, NF-κB, Wnt/β-catenin).
  • Examination of LRRC15 expression and function in the bone, joint, and tumor microenvironment.
  • Review of existing literature on LRRC15's association with skeletal diseases and osteosarcoma development.

Main Results:

  • LRRC15 mediates diverse cellular functions through transmembrane and intracellular signaling.
  • LRRC15 is implicated in the pathophysiology of osteoporosis, osteoarthritis, and rheumatoid arthritis.
  • LRRC15 is identified as a novel mesenchymal protein and a significant biomarker for osteosarcoma.

Conclusions:

  • LRRC15 is a key regulator of cellular interactions and immune responses with implications in skeletal health and disease.
  • Further understanding of LRRC15's role in the bone, joint, and tumor microenvironment is crucial.
  • LRRC15 presents a promising target for developing novel therapeutic strategies for skeletal diseases, including osteosarcoma.
Keywords:
LRRC15cell signalingextracellular matrixosteosarcomaskeletal biology

More Related Videos

Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate11:31

Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate

Published on: September 18, 2013

Assaying the Kinase Activity of LRRK2 in vitro06:09

Assaying the Kinase Activity of LRRK2 in vitro

Published on: January 18, 2012

Related Concept Videos

lncRNA - Long Non-coding RNAs02:39

lncRNA - Long Non-coding RNAs

In humans, more than 80% of the genome gets transcribed. However, only around 2% of the genome codes for proteins. The remaining part produces non-coding RNAs which includes ribosomal RNAs, transfer RNAs, telomerase RNAs, and regulatory RNAs, among other types. A large number of regulatory non-coding RNAs have been classified into two groups depending upon their length – small non-coding RNAs, such as microRNA, which are less than 200 nucleotides in length, and long non-coding RNA (lncRNA)...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
RNA Splicing01:32

RNA Splicing

Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...