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2016 ; 4
(ä): 124
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Septins As Modulators of Endo-Lysosomal Membrane Traffic
#MMPMID27857942
Song K
; Russo G
; Krauss M
Front Cell Dev Biol
2016[]; 4
(ä): 124
PMID27857942
show ga
Septins constitute a family of GTP-binding proteins, which assemble into
non-polar filaments in a nucleotide-dependent manner. These filaments can be
recruited to negatively charged membrane surfaces. When associated with membranes
septin filaments can act as diffusion barriers, which confine subdomains of
distinct biological functions. In addition, they serve scaffolding roles by
recruiting cytosolic proteins and other cytoskeletal elements. Septins have been
implicated in a large variety of membrane-dependent processes, including
cytokinesis, signaling, cell migration, and membrane traffic, and several family
members have been implicated in disease. However, surprisingly little is known
about the molecular mechanisms underlying their biological functions. This review
summarizes evidence in support of regulatory roles of septins during
endo-lysosomal sorting, with a particular focus on phosphoinositides, which serve
as spatial landmarks guiding septin recruitment to distinct subcellular
localizations.