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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Naked mole-rat TMEM2 lacks physiological hyaluronan-degrading activity.

Shinya Sato1, Yukiko Mizutani2, Minori Abe2

  • 1Department of Cosmetic Health Science, Gifu Pharmaceutical University, 1-25-4 Daigaku-nishi, Gifu, 501-1196, Japan; TOA Inc., Nippon Life Yodoyabashi Bldg., 17F, 3-5-29, Kitahama, Chuo-ku, Osaka, 541-0041, Japan.

Archives of Biochemistry and Biophysics
|July 15, 2024
PubMed
Summary

Mouse transmembrane protein 2 (mTMEM2) is a hyaluronidase, but human (hTMEM2) and naked mole-rat (nmrTMEM2) variants lack this activity due to specific amino acid differences. This inactivity in nmrTMEM2 may explain high-molecular-weight hyaluronan accumulation in naked mole-rats.

Keywords:
CEMIP2HYBIDHeterocephalus glaberHyaluronan depolymerizationHyaluronic acidHyaluronidase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Comparative Genomics

Background:

  • Transmembrane protein 2 (TMEM2) functions as a hyaluronidase, crucial for hyaluronan (HA) degradation.
  • Previous studies indicated human TMEM2 (hTMEM2) lacks catalytic activity due to absent key residues in its GG domain.
  • Naked mole-rats (NMRs) exhibit high levels of high-molecular-weight HA, suggesting impaired HA degradation.

Purpose of the Study:

  • To investigate the hyaluronan-degrading activity of naked mole-rat TMEM2 (nmrTMEM2).
  • To compare the enzymatic activity of nmrTMEM2 with mouse TMEM2 (mTMEM2) and hTMEM2.
  • To elucidate the role of specific amino acid residues in TMEM2 hyaluronidase function.

Main Methods:

  • Expression of mTMEM2, hTMEM2, and nmrTMEM2 in HEK293T cells.
  • Enzymatic assays using membrane fractions to assess HA-degrading activity.
  • Site-directed mutagenesis and chimeric protein construction to analyze critical amino acid residues.

Main Results:

  • nmrTMEM2, similar to hTMEM2, exhibited negligible HA-degrading activity.
  • Specific amino acid residues (Asn247/Val302 in nmrTMEM2; Asn248/Phe303 in hTMEM2) are critical for catalytic function.
  • Restoring the His248/Ala303 residues in a chimeric hTMEM2 construct restored catalytic activity.
  • Significantly higher concentrations of nmrTMEM2 and hTMEM2 were required to degrade HA compared to mTMEM2.

Conclusions:

  • nmrTMEM2 is not a physiological hyaluronidase, contrasting with mTMEM2.
  • The absence of critical residues in nmrTMEM2's GG domain renders it enzymatically inactive.
  • The impaired HA degradation by nmrTMEM2 likely contributes to the accumulation of high-molecular-weight HA in NMR tissues.