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Structural Insights into the Mechanism of Dynamin Superfamily Proteins.

ABSTRACT: Dynamin superfamily proteins (DSPs) mediate membrane fission and fusion necessary for endocytosis, organelle biogenesis and maintenance, as well as for bacterial cytokinesis. They also function in the innate immune response to pathogens and in organizing the cytoskeleton. In this review, we summarize the current understanding of the molecular mechanism of DSPs, with emphasis on the structural basis of function. Studies from the past decade on the structure and mechanism of DSPs enable comparative analysis of shared mechanisms and unique features of this protein family.

SUBMITTER: Jimah JR

PROVIDER: S-EPMC9623552 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

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Structural Insights into the Mechanism of Dynamin Superfamily Proteins.

Jimah John R JR Hinshaw Jenny E JE

Trends in cell biology 20181205 3

Dynamin superfamily proteins (DSPs) mediate membrane fission and fusion necessary for endocytosis, organelle biogenesis and maintenance, as well as for bacterial cytokinesis. They also function in the innate immune response to pathogens and in organizing the cytoskeleton. In this review, we summarize the current understanding of the molecular mechanism of DSPs, with emphasis on the structural basis of function. Studies from the past decade on the structure and mechanism of DSPs enable comparativ ...[more]

PMID: 30527453

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Project description:Recent advances in our structural understanding of telomerase and telomere-associated proteins have contributed significantly to elucidating the molecular mechanisms of telomere maintenance. The structures of telomerase TERT domains have provided valuable insights into how experimentally identified conserved motifs contribute to the telomerase reverse transcriptase reaction. Additionally, structures of telomere-associated proteins in a variety of organisms have revealed that, across evolution, telomere-maintenance mechanisms employ common structural elements. For example, the single-stranded 3' overhang of telomeric DNA is specifically and tightly bound by an OB-fold in nearly all species, including ciliates (TEBP and Pot1a), fission yeast (SpPot1), budding yeast (Cdc13), and humans (hPOT1). Structures of the yeast Cdc13, Stn1, and Ten1 proteins demonstrated that telomere maintenance is regulated by a complex that bears significant similarity to the RPA heterotrimer. Similarly, proteins that specifically bind double-stranded telomeric DNA in divergent species use homeodomains to execute their functions (human TRF1 and TRF2 and budding yeast ScRap1). Likewise, the conserved protein Rap1, which is found in budding yeast, fission yeast, and humans, contains a structural motif that is known to be critical for protein-protein interaction. In addition to revealing the common underlying themes of telomere maintenance, structures have also elucidated the specific mechanisms by which many of these proteins function, including identifying a telomere-specific domain in Stn1 and how the human TRF proteins avoid heterodimerization. In this review, we summarize the high-resolution structures of telomerase and telomere-associated proteins and discuss the emergent common structural themes among these proteins. We also address how these high-resolution structures complement biochemical and cellular studies to enhance our understanding of telomere maintenance and function.

Dataset Information

Structural Insights into the Mechanism of Dynamin Superfamily Proteins.

Publications

Structural Insights into the Mechanism of Dynamin Superfamily Proteins.

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