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Related Concept Videos

Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Cell Adhesion Molecules - Types and Functions01:20

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Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Adhesion01:14

Adhesion

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Adhesion occurs when one type of molecule is attracted to a different molecule. Water exhibits adhesive properties in the presence of polar surfaces, such as glass or cellulose in plants. For instance, when water is poured into a glass, the positively charged hydrogen molecules of water are more attracted to the negatively charged oxygen molecules in the silica than to the oxygen in neighboring water molecules.
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Adherens Junctions01:24

Adherens Junctions

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Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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Related Experiment Video

Updated: Mar 15, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Current research on adhesion regulating molecule 1: A Review.

Yiming Chen1, Tiantian Xu2, Tonghua Zhou3

  • 1College of Queen Mary, Nanchang University, Nanchang, Jiangxi Province, 330006, China.

Biochemical and Biophysical Research Communications
|March 13, 2026
PubMed
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Adhesion regulating molecule 1 (ADRM1) is a key protein linking degradation and signaling. Its overexpression drives cancer, but targeting it with inhibitors like RA190 shows anti-tumor potential.

Keywords:
ADRM1Cancer progressionProteasome

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Adhesion regulating molecule 1 (ADRM1), also known as regulatory particle non-ATPase subunit 13 (Rpn13), is a ubiquitin receptor crucial for proteasome function.
  • ADRM1 integrates protein degradation pathways with cellular signaling networks, influencing diverse biological processes.

Purpose of the Study:

  • To elucidate the multifaceted roles of ADRM1 in cellular functions, disease pathogenesis, and therapeutic strategies.
  • To highlight ADRM1's potential as a diagnostic biomarker and therapeutic target.

Main Methods:

  • Structural biology techniques to define ADRM1 domains (Pru and DEUBAD).
  • Analysis of ADRM1 interactions with proteins like Phg2, HDAC8, and PADI4.
  • Investigation of ADRM1's role in various cancers and physiological processes.
  • Identification and evaluation of small-molecule inhibitors targeting ADRM1.

Main Results:

  • ADRM1 coordinates substrate recognition and deubiquitination within the 26S proteasome.
  • Overexpression of ADRM1 is linked to proliferation, migration, metastasis, and therapeutic resistance in multiple cancers.
  • ADRM1 influences bone metabolism, reproduction, and immune regulation.
  • Small-molecule inhibitor RA190 selectively targets the ADRM1 Pru domain, demonstrating anti-tumor efficacy.

Conclusions:

  • ADRM1 is a critical molecular hub connecting proteasomal activity with signaling pathways.
  • ADRM1's oncogenic functions and physiological roles underscore its significance in health and disease.
  • Targeting ADRM1 presents a promising therapeutic avenue for various malignancies.