Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 21, Pages -Publisher
MDPI
DOI: 10.3390/ijms20215246
Keywords
AAA plus ATPase; peroxisome; PEX1; PEX6; PEX5; protein translocation
Funding
- 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
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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.
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