| First Author | Urade T | Year | 2014 |
| Journal | Kobe J Med Sci | Volume | 60 |
| Issue | 3 | Pages | E57-65 |
| PubMed ID | 25612671 | Mgi Jnum | J:227367 |
| Mgi Id | MGI:5700283 | Citation | Urade T, et al. (2014) Identification and characterization of TMEM33 as a reticulon-binding protein. Kobe J Med Sci 60(3):E57-65 |
| abstractText | Endoplasmic reticulum (ER) is an organelle that has an elaborate and continuous membrane system composed of sheet-like cisternae and a network of interconnected tubules. The ER tubules are shaped by reticulons, a conserved ER membrane protein family. However, how the membrane-shaping activity is regulated remains to be elucidated. To understand the mode of action of reticulons, we isolated TMEM33, a conserved protein harboring three transmembrane domains, as a reticulon 4C-binding protein by affinity chromatography. In addition to reticulon 4C, TMEM33 binds to reticulon 1A, -2B, -3C and a reticulon homology domain-containing protein Arl6IP1. Exogenously expressed TMEM33 localizes at both the ER membrane and the nuclear envelope. Exogenously expressed TMEM33 co-localizes with exogenously expressed reticulon 4C well at the ER sheets and partially at the ER tubules. Exogenously expressed TMEM33 suppresses the exogenously expressed reticulon 4C-induced tubulation of ER. These results suggest that TMEM33 has a potency to suppress the membrane-shaping activity of reticulons, thereby regulating the tubular structure of ER. |
