Septins in kidney: A territory little explored

Wasik, Anita A.; Dash, S. K.; Lehtonen, Sanna

doi:10.1002/cm.21477

Cited by 3 publications

(2 citation statements)

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“…These often associate with membranes in order to undertake their roles as molecular scaffolds, membrane modulators, and other cytoskeletal functions [1]. The current view of the septins shows that they are not simply passive molecules acting as scaffolds, but that they act in a physiologically regulated way [2]. Thus, it is not surprising that abnormalities in the expression and function of septins are associated with ageing, infectious diseases, neurodegenerative disorders, male infertility and even cancer [3].…”

Section: Graphical Abstract Introductionmentioning

confidence: 99%

Molecular Recognition at Septin Interfaces: The Switches Hold the Key

Rosa

Leonardo

Brognara

et al. 2020

Journal of Molecular Biology

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The assembly of a septin filament requires that homologous monomers must distinguish between one another in establishing appropriate interfaces with their neighbours. To understand this phenomenon at the molecular level, we present the first four crystal structures of heterodimeric septin complexes. We describe in detail the two distinct types of G-interface present within the octameric particles which must polymerize to form filaments. These are formed between SEPT2 and SEPT6 and between SEPT7 and SEPT3, and their description permits an understanding of the structural basis for the selectivity necessary for correct filament assembly. By replacing SEPT6 by SEPT8 or SEPT11, it is possible to rationalize Kinoshita´s postulate which predicts the exchangeability of septins from within a subgroup. Switches I and II, which in classical small GTPases provide a mechanism for nucleotide-dependent conformational change, have been repurposed in septins to play a fundamental role in molecular recognition. Specifically, it is switch I which holds the key to discriminating between the two different G-interfaces. Moreover, residues which are characteristic for a given subgroup play subtle, but pivotal, roles in guaranteeing that the correct interfaces are formed.

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Section: Graphical Abstract Introductionmentioning

confidence: 99%

Molecular Recognition at Septin Interfaces: The Switches Hold the Key

Rosa

Leonardo

Brognara

et al. 2020

Journal of Molecular Biology

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“…Neubauer et al show using immunohistochemistry and RTPCR that septin expression is significantly upregulated in fibrotic kidney (Neubauer et al, 2018b). Moreover, Wasik et al report that Sept7b knockdown in zebrafish results in damaged pronephros and defective cilia formation (Wasik et al, 2018). These two studies will hopefully lead to future studies concerning septin function in the kidney.…”

mentioning

confidence: 98%

Editorial overview: The molecular and cellular biology of septins

Mostowy

Ewers

2019

Cytoskeleton

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This Septins Special Issue of Cytoskeleton addresses fundamental aspects of septin structure, assembly and function. The group of 18 articles has been inspired by the recent European Molecular Biology Organization (EMBO) Workshop entitled 'Molecular and Cellular Biology of Septins' held in Berlin, Germany, on October 8-11, 2017, furthe r described in a recent meeting report (Caudron and Yadav, 2018).

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Molecular recognition at septin interfaces: the switches hold the key

Rosa

Leonardo

Brognara

et al. 2020

Preprint

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ABSTRACTThe assembly of a septin filament requires that homologous monomers must distinguish between one another in establishing appropriate interfaces with their neighbours. To understand this phenomenon at the molecular level, we present the first four crystal structures of heterodimeric septin complexes. We describe in detail the two distinct types of G-interface present within the octameric particles which must polymerize to form filaments. These are formed between SEPT2 and SEPT6 and between SEPT7 and SEPT3, and their description permits an understanding of the structural basis for the selectivity necessary for correct filament assembly. By replacing SEPT6 by SEPT8 or SEPT11, it is possible to rationalize Kinoshita’s postulate which predicts the exchangeability of septins from within a subgroup. Switches I and II, which in classical small GTPases provide a mechanism for nucleotide-dependent conformational change, have been repurposed in septins to play a fundamental role in molecular recognition. Specifically, it is switch I which holds the key to discriminating between the two different G-interfaces. Moreover, residues which are characteristic for a given subgroup play subtle, but pivotal, roles in guaranteeing that the correct interfaces are formed.HIGHLIGHTSHigh resolution structures of septin heterodimeric complexes reveal new interactionsSwitches of small GTPases are repurposed in septins to play key roles in interface contactsThe GTP present in catalytically inactive septins participates in molecular recognitionConservation of interface residues allows for subunit exchangeability from within septin subgroupsSpecific residues for each septin subgroup provide selectivity for proper filament assemblyGRAPHICAL ABSTRACT

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Septins in kidney: A territory little explored

Cited by 3 publications

References 79 publications

Molecular Recognition at Septin Interfaces: The Switches Hold the Key

Molecular Recognition at Septin Interfaces: The Switches Hold the Key

Editorial overview: The molecular and cellular biology of septins

Molecular recognition at septin interfaces: the switches hold the key

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