期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 20, 期 21, 页码 -出版社
MDPI
DOI: 10.3390/ijms20215246
关键词
AAA plus ATPase; peroxisome; PEX1; PEX6; PEX5; protein translocation
资金
- FEDER-Fundo Europeu de Desenvolvimento Regional funds through the COMPETE 2020-Operacional Programme for Competitiveness and Internationalisation (POCI), Portugal 2020
- Portuguese funds through FCT-Fundacao para a Ciencia e a Tecnologia/Ministerio da Ciencia, Tecnologia e Ensino Superior [PTDC/BEX-BCM/2311/2014 (POCI-01-0145-FEDER-016613), POCI-01-0145-FEDER-007274]
- Norte Portugal Regional Operational Programme (NORTE 2020), under the PORTUGAL 2020 Partnership Agreement, through the European Regional Development Fund (FEDER) [NORTE-01-0145-FEDER-000008]
- Fundacao para a Ciencia e Tecnologia
- Programa Operacional Potencial Humano do QREN
- Fundo Social Europeu
In contrast to many protein translocases that use ATP or GTP hydrolysis as the driving force to transport proteins across biological membranes, the peroxisomal matrix protein import machinery relies on a regulated self-assembly mechanism for this purpose and uses ATP hydrolysis only to reset its components. The ATP-dependent protein complex in charge of resetting this machinery-the Receptor Export Module (REM)-comprises two members of the ATPases Associated with diverse cellular Activities (AAA+) family, PEX1 and PEX6, and a membrane protein that anchors the ATPases to the organelle membrane. In recent years, a large amount of data on the structure/function of the REM complex has become available. Here, we discuss the main findings and their mechanistic implications.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据