Setting the F-BAR: Functions and regulation of the F-BAR protein family

Roberts-Galbraith, Rachel H.; Gould, Kathleen L.

doi:10.4161/cc.9.20.13587

Cited by 74 publications

(87 citation statements)

References 67 publications

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“…On one hand, Dbf2p and Mob1p have been found at the actin-myosin ring (AMR) structure that is essential for abscission [35][36][37][38], and Cdc15p, Dbf2p and Mob1p are required for AMR contraction [39,40]. Moreover, current evidence suggests that the MEN components Dbf2p and Mob1p can regulate the cytokinetic components Chs2p, Hof1p, and Inn1p (summarised in [33,41]). However, Hof1p (one of at least three F-BAR domain proteins in S. cerevisiae) is so far the only established target of Mob1p/Dbf2p in cytokinesis [41].…”

Section: Mitotic Exit Network (Men) In S Cerevisiaementioning

confidence: 99%

“…Moreover, current evidence suggests that the MEN components Dbf2p and Mob1p can regulate the cytokinetic components Chs2p, Hof1p, and Inn1p (summarised in [33,41]). However, Hof1p (one of at least three F-BAR domain proteins in S. cerevisiae) is so far the only established target of Mob1p/Dbf2p in cytokinesis [41].…”

Section: Mitotic Exit Network (Men) In S Cerevisiaementioning

confidence: 99%

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Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

Hergovich

Hemmings

2012

Seminars in Cell & Developmental Biology

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Over the past decade Hippo kinase signalling has been established as an essential tumour suppressor pathway controlling tissue growth in flies and mammals. All members of the Hippo core signalling cassette are conserved from yeast to humans, whereby the yeast analogues of Hippo, Mats and Lats are central components of the mitotic exit network and septation initiation network in budding and fission yeast, respectively. Here, we discuss how far core Hippo signalling components in Drosophila melanogaster and mammals have reported similar mitotic functions as already established for their highly conserved yeast counterparts.

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Section: Mitotic Exit Network (Men) In S Cerevisiaementioning

confidence: 99%

Section: Mitotic Exit Network (Men) In S Cerevisiaementioning

confidence: 99%

Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

Hergovich

Hemmings

2012

Seminars in Cell & Developmental Biology

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“…In support of this model, phosphoregulation of F-BAR-and SH3-domain-containing proteins is emerging as a common mechanism to modulate the conformation, subcellular localization, and activity of proteins that contain these domains (38). A striking difference between these proteins and Pacsin1, however, is that phosphorylation inhibits their association with known ligands while phosphorylation of Pacsin1 appears to promote its interaction with a known binding partner.…”

Section: Discussionmentioning

confidence: 98%

Identification of neuronal substrates implicates Pak5 in synaptic vesicle trafficking

Strochlic

Concilio

Viaud

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Synaptic transmission is mediated by a complex set of molecular events that must be coordinated in time and space. While many proteins that function at the synapse have been identified, the signaling pathways regulating these molecules are poorly understood. Pak5 (p21-activated kinase 5) is a brain-specific isoform of the group II Pak kinases whose substrates and roles within the central nervous system are largely unknown. To gain insight into the physiological roles of Pak5, we engineered a Pak5 mutant to selectively radiolabel its substrates in murine brain extract. Using this approach, we identified two novel Pak5 substrates, Pacsin1 and Synaptojanin1, proteins that directly interact with one another to regulate synaptic vesicle endocytosis and recycling. Pacsin1 and Synaptojanin1 were phosphorylated by Pak5 and the other group II Paks in vitro, and Pak5 phosphorylation promoted Pacsin1-Synaptojanin1 binding both in vitro and in vivo. These results implicate Pak5 in Pacsin1-and Synaptojanin1-mediated synaptic vesicle trafficking and may partially account for the cognitive and behavioral deficits observed in group II Pak-deficient mice.

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“…The membrane invagination stage is regulated by the strict cooperation between the cytoskeleton, phospholipids and amphipathic membrane proteins, which often contain BAR domains that protrude from the cytoplasmic face of the membrane (reviewed by Roberts-Galbraith and Gould, 2010;Suetsugu and Gautreau, 2012). In clathrin-mediated invaginations, amphiphysin and endophilin are examples of such amphipathic proteins (Fütterer and Machesky, 2007).…”

Section: Sculpting Of Membrane Invaginationsmentioning

confidence: 99%

“…It has been shown that, in order to induce protrusions and invaginations of the cell surface, remodeling of the cytoskeleton requires the cooperation of membrane-associated components, such as amphipathic proteins, which often contain membranedeforming Bin-amphiphysin-Rys (BAR) domains (reviewed by Graham and Kozlov, 2010;Roberts-Galbraith and Gould, 2010;Suetsugu and Gautreau, 2012). Furthermore, the cortical cytoskeleton, which previously was considered primarily as a barrier, was recognized as also having a positive role in the surface traffic of vesicles (reviewed by Momboisse et al, 2010;Villanueva et al, 2012;Nightingale et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Cell surface dynamics – how Rho GTPases orchestrate the interplay between the plasma membrane and the cortical cytoskeleton

Curtis

Meldolesi

2012

Journal of Cell Science

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SummarySmall GTPases are known to regulate hundreds of cell functions. In particular, Rho family GTPases are master regulators of the cytoskeleton. By regulating actin nucleation complexes, Rho GTPases control changes in cell shape, including the extension and/or retraction of surface protrusions and invaginations. Protrusion and invagination of the plasma membrane also involves the interaction between the plasma membrane and the cortical cytoskeleton. This interplay between membranes and the cytoskeleton can lead to an increase or decrease in the plasma membrane surface area and its tension as a result of the fusion (exocytosis) or internalization (endocytosis) of membranous compartments, respectively. For a long time, the cytoskeleton and plasma membrane dynamics were investigated separately. However, studies from many laboratories have now revealed that Rho GTPases, their modulation of the cytoskeleton, and membrane traffic are closely connected during the dynamic remodeling of the cell surface. Arf-and Rab-dependent exocytosis of specific vesicles contributes to the targeting of Rho GTPases and their regulatory factors to discrete sites of the plasma membrane. Rho GTPases regulate the tethering of exocytic vesicles and modulate their subsequent fusion. They also have crucial roles in the different forms of endocytosis, where they participate in the sorting of membrane domains as well as the sculpting and sealing of membrane flasks and cups. Here, we discuss how cell surface dynamics depend on the orchestration of the cytoskeleton and the plasma membrane by Rho GTPases.

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Setting the F-BAR: Functions and regulation of the F-BAR protein family

Cited by 74 publications

References 67 publications

Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

Identification of neuronal substrates implicates Pak5 in synaptic vesicle trafficking

Cell surface dynamics – how Rho GTPases orchestrate the interplay between the plasma membrane and the cortical cytoskeleton

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