Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP

Zhang, Jianshe; Chen, Kong; Xie, Hui; McPherson, Peter S.; Grinstein, Sergio; Trimble, William S.

doi:10.1016/s0960-9822(00)80115-3

Cited by 289 publications

(317 citation statements)

References 42 publications

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“…N-terminal to the GTP-binding domain is a phosphoinositide-binding motif ( Figure 1a) [35,36], and plasma membrane phosphatidylinositol (4,5)-bisphosphate is important for the maintenance of proper septin architecture in vivo [37]. To the C-terminal side, there is a highly conserved sequence of unknown function that is unique to and a hallmark of septins.…”

Section: Assembly Of Hetero-oligomeric Multi-septin Complexes In Buddmentioning

confidence: 99%

Some assembly required: yeast septins provide the instruction manual

Versele

Thorner

2005

Trends in Cell Biology

200

199

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Septins are a family of conserved proteins that form hetero-oligomeric complexes that assemble into filaments. The filaments can be organized into linear arrays, coils, rings and gauzes. They serve as membrane-associated scaffolds and as barriers to demarcate local compartments, especially for the establishment of the septation site for cytokinesis. Studies in budding and fission yeast have revealed many of the protein-protein interactions that govern the formation of multi-septin complexes. GTP binding and phosphorylation direct the polymerization of filaments that is required for septin-collar assembly in budding yeast, whereas a homolog of anillin instructs timely formation of the ring of septin filaments at the medial cortex in fission yeast. These insights should aid understanding of the organization and function of the diverse septin structures in animal cells.

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Section: Assembly Of Hetero-oligomeric Multi-septin Complexes In Buddmentioning

confidence: 99%

Some assembly required: yeast septins provide the instruction manual

Versele

Thorner

2005

Trends in Cell Biology

200

199

View full text Add to dashboard Cite

show abstract

“…G154V has a missense mutation in its "P-loop" domain and shows reduced guanine nucleotide-binding activity (21,28,35). The transfected cells were lysed in a buffer containing 1% Nonidet P-40, and the subcellular components were separated into Nonidet P-40-soluble and -insoluble fractions.…”

Section: Sept4/h5 In Lewy Bodiesmentioning

confidence: 99%

Association of the Cytoskeletal GTP-binding Protein Sept4/H5 with Cytoplasmic Inclusions Found in Parkinson's Disease and Other Synucleinopathies

Ihara

Tomimoto

Kitayama

et al. 2003

Journal of Biological Chemistry

128

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␣-Synuclein-positive cytoplasmic inclusions are a pathological hallmark of several neurodegenerative disorders including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Here we report that Sept4, a member of the septin protein family, is consistently found in these inclusions, whereas five other septins (Sept2, Sept5, Sept6, Sept7, and Sept8) are not found in these inclusions. Sept4 and ␣-synuclein can also be co-immunoprecipitated from normal human brain lysates. When co-expressed in cultured cells, FLAG-tagged Sept4 and Myc-tagged ␣-synuclein formed detergent-insoluble complex, and upon treatment with a proteasome inhibitor, they formed Lewy body-like cytoplasmic inclusions. The tagged Sept4 and ␣-synuclein synergistically accelerated cell death induced by the proteasome inhibitor, and this effect was further enhanced by expression of another Lewy body-associated protein, synphilin-1, tagged with the V5 epitope. Moreover, co-expression of the three proteins (tagged Sept4, ␣-synuclein, and synphilin-1) was sufficient to induce cell death. These data raise the possibility that Sept4 is involved in the formation of cytoplasmic inclusions as well as induction of cell death in ␣-synuclein-associated neurodegenerative disorders.

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“…Besides the elimination of aberrant or truncated proteins for cellular housekeeping, this pathway regulates the amount of active proteins, which depends on the synthesis/degradation ratio. An example is the human PARKIN protein, involved in autosomal recessive familial Parkinson's disease, which functions as E3 ligase promoting the degradation of a synaptic vesicle-associated septin [1,2]. Furthermore, other regulatory functions (i.e.…”

Section: Introductionmentioning

confidence: 99%

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

Mazzucotelli

Belloni²,

Marone³

et al. 2006

238

178

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Abstract:The regulation of protein expression and activity has been for long time considered only in terms of transcription/translation efficiency. In the last years, the discovery of post-transcriptional and post-translational regulation mechanisms pointed out that the key factor in determining transcript/protein amount is the synthesis/degradation ratio, together with post-translational modifications of proteins. Polyubiquitinaytion marks target proteins directed to degradation mediated by 26S-proteasome. Recent functional genomics studies pointed out that about 5% of Arabidopsis genome codes for proteins of ubiquitination pathway. The most of them (more than one thousand genes) correspond to E3 ubiquitin ligases that specifically recognise target proteins. The huge size of this gene family, whose members are involved in regulation of a number of biological processes including hormonal control of vegetative growth, plant reproduction, light response, biotic and abiotic stress tolerance and DNA repair, indicates a major role for protein degradation in control of plant life.

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Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP

Abstract: These results indicate that the interaction of septins with PtdInsP(2) might be an important cellular mechanism for the spatial and temporal control of septin accumulation.

Cited by 289 publications

References 42 publications

Some assembly required: yeast septins provide the instruction manual

Some assembly required: yeast septins provide the instruction manual

Association of the Cytoskeletal GTP-binding Protein Sept4/H5 with Cytoplasmic Inclusions Found in Parkinson's Disease and Other Synucleinopathies

The E3 Ubiquitin Ligase Gene Family in Plants: Regulation by Degradation

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