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ナカムラ ノブヒロ
NAKAMURA NOBUHIRO
中村 暢宏 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2002 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Differential recognition of tyrosine-based basolateral signals by AP-1B subunit μ1B in polarized epithelial cells |
| 執筆形態 | その他 |
| 掲載誌名 | Molecular Biology of the Cell |
| 出版社・発行元 | AMER SOC CELL BIOLOGY |
| 巻・号・頁 | 13(7),pp.2374-2382 |
| 著者・共著者 | Sugimoto, H.,Sugahara, M.,Fölsch, H.,Koide, Y.,Nakatsu, F.,Tanaka, N.,Nishimura, T.,Furukawa, M.,Mullins, C.,Nakamura, N.,Mellman, I.,Ohno, H. |
| 概要 | To investigate the importance of tyrosine recognition by the AP-1B clathrin adaptor subunit mu1B for basolateral sorting of integral membrane proteins in polarized epithelial cells, we have produced and characterized a mutant form of mu1B. The mutant (M-mu1B) contains alanine substitutions of each of the four conserved residues, which in the AP-2 adaptor subunit mu2 are critical for interacting with tyrosine-based endocytosis signals. We show M-mu1B is defective for tyrosine binding in vitro, but is nevertheless incorporated into AP-1 complexes in transfected cells. Using LLC-PK1 cells expressing either wild type or M-mu1B, we find that there is inefficient basolateral expression of membrane proteins whose basolateral targeting signals share critical tyrosines with signals for endocytosis. In contrast, membrane proteins whose basolateral targeting signals are distinct from their endocytosis signals (transferrin and low-density lipoprotein receptors) accumulate at the basolateral domain normally, although in a manner that is strictly dependent on mu1B or M-mu1B expression. Our results suggest that mu1B interacts with different classes of basolateral targeting signals in distinct ways. |
| DOI | 10.1091/mbc.E01-10-0096 |
| ISSN | 1059-1524 |
| Put Code(ORCID) | 19809416 |