BSD: a novel domain in transcription factors and synapse-associated proteins

Doerks, Tobias; Huber, Saskia; Buchner, Erich; Bork, Peer

doi:10.1016/s0968-0004(01)02042-4

Cited by 36 publications

(37 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Synapseassociated proteins are expressed specifically in neurons and act as important molecular elements of the nervous system [22,24]. Here, we show that this protein is down-regulated in the head of sporozoite-infected Anopheles (Table 2).…”

Section: Synaptic Transmissionmentioning

confidence: 59%

“…Multiple cellular processes such as structural organization of the cell, intra-cellular signalling by enzyme modulation, ion flux, growth control and atypical calcium channel [33] a) The scores of up-/down-regulation are derived from the average ratio of the normalised spot volumes in S1: Mf, Mg in Table 2) in the head of sporozoite-infected mosquitoes indicates a possible alteration in neuronal functioning [24]. In addition, since tropomyosins are involved in neuronal morphogenesis [30,44], the variation in cytoarchitectural proteins shown here (spots Me and Mk) may trigger structural changes in the Anopheles CNS and hence may warrant further investigations into the effect of an altered cytoskeleton.…”

Section: (111) Annexinmentioning

confidence: 99%

See 1 more Smart Citation

Malaria Plasmodium agent induces alteration in the head proteome of their Anopheles mosquito host

et al. 2007

View full text Add to dashboard Cite

Despite increasing evidence of behavioural manipulation of their vectors by pathogens, the underlying mechanisms causing infected vectors to act in ways that benefit pathogen transmission remain enigmatic in most cases. Here, 2-D DIGE coupled with MS were employed to analyse and compare the head proteome of mosquitoes (Anopheles gambiae sensu stricto (Giles)) infected with the malarial parasite (Plasmodium berghei) with that of uninfected mosquitoes. This approach detected altered levels of 12 protein spots in the head of mosquitoes infected with sporozoites. These proteins were subsequently identified using MS and functionally classified as belonging to metabolic, synaptic, molecular chaperone, signalling, and cytoskeletal groups. Our results indicate an altered energy metabolism in the head of sporozoite-infected mosquitoes. Some of the up-/down-regulated proteins identified, such as synapse-associated protein, 14-3-3 protein and calmodulin, have previously been shown to play critical roles in the CNS of both invertebrates and vertebrates. Furthermore, a heat shock response (HSP 20) and a variation of cytoarchitecture (tropomyosins) have been shown. Discovery of these proteins sheds light on potential molecular mechanisms that underlie behavioural modifications and offers new insights into the study of intimate interactions between Plasmodium and its Anopheles vector.

show abstract

Section: Synaptic Transmissionmentioning

confidence: 59%

Section: (111) Annexinmentioning

confidence: 99%

Malaria Plasmodium agent induces alteration in the head proteome of their Anopheles mosquito host

et al. 2007

View full text Add to dashboard Cite

show abstract

“…Our initial analysis identified six subgroups based on additional shared domains or motifs: BTB proteins that contain a MATH domain (Uren and Vaux, 1996), BTB proteins that contain a BTB domain as the only recognizable domain (Ahmad et al, 1998), BTB proteins that contain an ankyrin repeat (Kohl et al, 2003), BTB proteins that contain a TAZ zinc finger domain (De Guzman et al, 2000), BTB proteins that contain an armadillo/b-catenin-like repeat (Huber et al, 1997), and BTB proteins that contain a BSD domain (Doerks et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

Arabidopsis Has Two Redundant Cullin3 Proteins That Are Essential for Embryo Development and That Interact with RBX1 and BTB Proteins to Form Multisubunit E3 Ubiquitin Ligase Complexes in Vivo

et al. 2005

View full text Add to dashboard Cite

Cullin-based E3 ubiquitin ligases play important roles in the regulation of diverse developmental processes and environmental responses in eukaryotic organisms. Recently, it was shown in Schizosaccharomyces pombe, Caenorhabditis elegans, and mammals that Cullin3 (CUL3) directly associates with RBX1 and BTB domain proteins in vivo to form a new family of E3 ligases, with the BTB protein subunit functioning in substrate recognition. Here, we demonstrate that Arabidopsis thaliana has two redundant CUL3 (AtCUL3) genes that are essential for embryo development. Besides supporting anticipated specific AtCUL3 interactions with the RING protein AtRBX1 and representative Arabidopsis proteins containing a BTB domain in vitro, we show that AtCUL3 cofractionates and specifically associates with AtRBX1 and a representative BTB protein in vivo. Similar to the AtCUL1 subunit of the SKP1-CUL1-F-box protein-type E3 ligases, the AtCUL3 subunit of the BTB-containing E3 ligase complexes is subjected to modification and possible regulation by the ubiquitin-like protein Related to Ubiquitin in vivo. Together with the presence of large numbers of BTB proteins with diverse structural features and expression patterns, our data suggest that Arabidopsis has conserved AtCUL3-RBX1-BTB protein E3 ubiquitin ligases to target diverse protein substrates for degradation by the ubiquitin/proteasome pathway.

show abstract

“…The BSD domain is localized in a conserved central region and is found in BTF2-like transcription factors, SAP47 homolog proteins, and DOS2-like proteins. The domain is characterized by three predicted ␣ helices and a conserved phenylalanine-tryptophan amino acid pair (Doerks et al, 2002). SAP47 is abundant in synaptic terminals (Reichmuth et al, 1995;Funk et al, 2004), but a role in synaptic function and/or behavior has not been determined, in any species.…”

Section: Introductionmentioning

confidence: 99%

Behavioral and Synaptic Plasticity Are Impaired upon Lack of the Synaptic Protein SAP47

Saumweber¹,

Weyhersmüller²,

Hallermann³

et al. 2011

J. Neurosci.

View full text Add to dashboard Cite

The synapse-associated protein of 47 kDa (SAP47) is a member of a phylogenetically conserved gene family of hitherto unknown function. In Drosophila, SAP47 is encoded by a single gene (Sap47) and is expressed throughout all synaptic regions of the wild-type larval brain; specifically, electron microscopy reveals anti-SAP47 immunogold labeling within 30 nm of presynaptic vesicles. To analyze SAP47 function, we used the viable and fertile deletion mutant Sap47 156 , which suffers from a 1.7 kb deletion in the regulatory region and the first exon. SAP47 cannot be detected by either immunoblotting or immunohistochemistry in Sap47 156 mutants. These mutants exhibit normal sensory detection of odorants and tastants as well as normal motor performance and basic neurotransmission at the neuromuscular junction. However, short-term plasticity at this synapse is distorted. Interestingly, Sap47 156 mutant larvae also show a 50% reduction in odorant-tastant associative learning ability; a similar associative impairment is observed in a second deletion allele (Sap47 201 ) and upon reduction of SAP47 levels using RNA interference. In turn, transgenically restoring SAP47 in Sap47 156 mutant larvae rescues the defect in associative function. This report thus is the first to suggest a function for SAP47. It specifically argues that SAP47 is required for proper behavioral and synaptic plasticity in flies-and prompts the question whether its homologs are required for proper behavioral and synaptic plasticity in other species as well.

show abstract

BSD: a novel domain in transcription factors and synapse-associated proteins

Cited by 36 publications

References 12 publications

Malaria Plasmodium agent induces alteration in the head proteome of their Anopheles mosquito host

Malaria Plasmodium agent induces alteration in the head proteome of their Anopheles mosquito host

Arabidopsis Has Two Redundant Cullin3 Proteins That Are Essential for Embryo Development and That Interact with RBX1 and BTB Proteins to Form Multisubunit E3 Ubiquitin Ligase Complexes in Vivo

Behavioral and Synaptic Plasticity Are Impaired upon Lack of the Synaptic Protein SAP47

Contact Info

Product

Resources

About