ArticleThe international journal of biochemistry & cell biology2009
Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.
Article in The international journal of biochemistry & cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Mgr2 regulates mitochondrial preprotein import by associating with channel-forming Tim23 subunit.Molecular biology of the cell · 2020Article
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- Article
- Two distinct membrane potential-dependent steps drive mitochondrial matrix protein translocation.The Journal of cell biology · 2017Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Architecture of the TIM23 inner mitochondrial translocon and interactions with the matrix import motor.The Journal of biological chemistry · 2014Article
- Sequential duplications of an ancient member of the DnaJ-family expanded the functional chaperone network in the eukaryotic cytosol.Molecular biology and evolution · 2013Article
- Signal recognition initiates reorganization of the presequence translocase during protein import.The EMBO journal · 2013Article
- Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae.Genetics · 2012Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Import of proteins into the matrix is driven by the Tim23 presequence translocase-associated import motor PAM. The core component of PAM is the mitochondrial chaperone mtHsp70, which ensures efficient translocation of proteins across the inner membrane through interactions with the J-protein complex Pam16-Pam18 (Tim16-Tim14) and its cochaperone Tim44. The recently identified non-essential Pam17 is a further member of PAM. Genetic and biochemical analyses reveal synthetic interactions between PAM17 and TIM44. Pam17 is involved in an early stage of protein translocation whereas Tim44 assists in a later step of transport, suggesting that both proteins can cooperate in a complementary manner in protein import.
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Registered trials
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