3X23

Radixin complex

Summary for 3X23

• Entry DOI: 10.2210/pdb3x23/pdb
• Related: 1GC6 1GC7 1ISN 1J19 2D10 2D11 2D2Q 2EMS 2EMT 2YVC 2ZPY
• Descriptor: Radixin, Peptide from Matrix metalloproteinase-14 (3 entities in total)
• Functional Keywords: ferm domain, cell adhesion, adhesion receptors, cell invasion
• Biological source: Mus musculus (mouse); More
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043; Membrane ; Single-pass type I membrane protein : P50281
• Total number of polymer chains: 2
• Total formula weight: 39399.51

Authors

Terawaki, S.,Kitano, K.,Aoyama, M.,Mori, T.,Hakoshima, T. (deposition date: 2014-12-09, release date: 2015-10-21, Last modification date: 2023-11-08)

Primary citation

Terawaki, S.,Kitano, K.,Aoyama, M.,Mori, T.,Hakoshima, T.
MT1-MMP recognition by ERM proteins and its implication in CD44 shedding
Genes Cells, 20:847-859, 2015

PubMed Abstract: Membrane type 1-matrix metalloproteinase (MT1-MMP) is a key enzyme involved in tumor cell invasion by shedding their cell-surface receptor CD44 anchored with F-actin through ezrin/radixin/moesin (ERM) proteins. We found the cytoplasmic tail of MT1-MMP directly binds the FERM domain of radixin, suggesting F-actin-based recruitment of MT1-MMP to CD44 for invasion. Our crystal structure shows that the central region of the MT1-MMP cytoplasmic tail binds subdomain A of the FERM domain, and makes an antiparallel β-β interaction with β2A-strand. This binding mode is distinct from the previously determined binding mode of CD44 to subdomain C. We showed that radixin simultaneously binds both MT1-MMP and CD44, indicating ERM protein-mediated colocalization of MT1-MMP and its substrate CD44 and anchoring to F-actin. Our study implies that ERM proteins contribute toward accelerated CD44 shedding by MT1-MMP through ERM protein-mediated interactions between their cytoplasmic tails.

PubMed: 26289026
DOI: 10.1111/gtc.12276

Experimental method

X-RAY DIFFRACTION (2.396 Å)