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1.
Anne Berna François Bernier Eric Chabrière Mikael Elias Ken Scott Andrew Suh 《Cellular and molecular life sciences : CMLS》2009,66(14):2205-2218
DING proteins, identified mainly by their eponymous N-terminal sequences, are ubiquitous in living organisms. Amongst bacteria,
they are common in pseudomonads, and have been characterised with respect to genetics and structure. They form part of a wider
family of phosphate-binding proteins, with emerging roles in phosphate acquisition and pathogenicity. Many DING proteins have
been isolated in eukaryotes, in which they have been associated with very diverse biological activities, often in the context
of possible signalling roles. Disease states in which DING proteins have been implicated include rheumatoid arthritis, lithiasis,
atherosclerosis, some tumours and tumour-associated cachexia, and bacterial and viral adherence. Complete genetic and structural
characterisation of eukaryotic DING genes and proteins is still lacking, though the phosphate-binding site seems to be conserved.
Whether as bacterial proteins related to bacterial pathogenicity, or as eukaryotic components of biochemical signalling systems,
DING proteins require further study.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. 相似文献
2.
The BAG (Bcl-2 associated athanogene) family is a multifunctional group of proteins that perform diverse functions ranging from apoptosis to tumorigenesis.
An evolutionarily conserved group, these proteins are distinguished by a common conserved region known as the BAG domain.
BAG genes have been found in yeasts, plants, and animals, and are believed to function as adapter proteins forming complexes
with signaling molecules and molecular chaperones. In humans, a role for BAG proteins has been suggested in carcinogenesis,
HIV infection, and Parkinson’s disease. These proteins are therefore potential therapeutic targets, and their expression in
cells may serve as a predictive tool for such diseases. In plants, the Arabidopsis thaliana genome contains seven homologs of the BAG family, including four with domain organization similar to animal BAGs. Three members
contain a calmodulin-binding domain possibly reflecting differences between plant and animal programmed cell death. This review
summarizes current understanding of BAG proteins in both animals and plants.
Received 21 November 2007; received after revision 17 December 2007; accepted 2 January 2008 相似文献
3.
Rob Houtmeyers Jacob Souopgui Sabine Tejpar Ruth Arkell 《Cellular and molecular life sciences : CMLS》2013,70(20):3791-3811
The zinc finger of the cerebellum gene (ZIC) discovered in Drosophila melanogaster (odd-paired) has five homologs in Xenopus, chicken, mice, and humans, and seven in zebrafish. This pattern of gene copy expansion is accompanied by a divergence in gene and protein structure, suggesting that Zic family members share some, but not all, functions. ZIC genes are implicated in neuroectodermal development and neural crest cell induction. All share conserved regions encoding zinc finger domains, however their heterogeneity and specification remain unexplained. In this review, the evolution, structure, and expression patterns of the ZIC homologs are described; specific functions attributable to individual family members are supported. A review of data from functional studies in Xenopus and murine models suggest that ZIC genes encode multifunctional proteins operating in a context-specific manner to drive critical events during embryogenesis. The identification of ZIC mutations in congenital syndromes highlights the relevance of these genes in human development. 相似文献
4.
Matthew D. Hitchings Philip Townsend Ehmke Pohl Paul D. Facey D. Hugh Jones Paul J. Dyson Ricardo Del Sol 《Cellular and molecular life sciences : CMLS》2014,71(24):4911-4926
Dps proteins are members of an extensive family of proteins that oxidise and deposit iron in the form of ferric oxide, and are also able to bind DNA. Ferroxidation centres are formed at the interface of anti-parallel dimers, which further assemble into dodecameric nanocages with a hollow core where ferric oxide is deposited. Streptomyces coelicolor encodes three Dps-like proteins (DpsA, B and C). Despite sharing the conserved four-helix bundle organisation observed in members of the Dps family, they display significant differences in the length of terminal extensions, or tails. DpsA possess both N- and C-terminal tails of different lengths, and their removal affects quaternary structure assembly to varying degrees. DpsC quaternary structure, on the other hand, is heavily dependent on its N-terminal tail as its removal abolishes correct protein folding. Analysis of the crystal structure of dodecamers from both proteins revealed remarkable differences in the position of tails and interface surface area; and provides insight to explain the differences in biochemical behaviour observed while comparing DpsA and DpsC. 相似文献
5.
Wang Y Guan X Fok KL Li S Zhang X Miao S Zong S Koide SS Chan HC Wang L 《Cellular and molecular life sciences : CMLS》2008,65(23):3822-3829
Rhomboid family members are widely conserved and found in all three kingdoms of life. They are serine proteases and serve
important regulatory functions. In the present study, a novel gene highly expressed in the testis, RHBDD1, is shown to be
a new member of the Rhomboid family, participating in the cleavage of BIK, a proapoptotic member of the Bcl-2 family. The
RHBDD1-involved proteolytic modification is upstream of the BIK protein degradation pathway. Mutagenesis studies show that
the amino acid residues glycine142 and serine144 of RHBDD1 are crucial for its activity in cleaving BIK at a site located
in the transmembrane region. Overexpression or knock-down of RHBDD1 in HEK 293T cells can reduce or enhance BIK-mediated apoptosis,
respectively. The present findings suggest that, by acting as a serine protease, RHBDD1 modulates BIK-mediated apoptotic activity.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.
Received 31 July 2008; received after revision 16 September 2008; accepted 19 September 2008 相似文献
6.
The multifunctional roles of the four-and-a-half-LIM only protein FHL2 总被引:15,自引:1,他引:14
Johannessen M Møller S Hansen T Moens U Van Ghelue M 《Cellular and molecular life sciences : CMLS》2006,63(3):268-284
7.
Matricellular proteins interact with the extracellular matrix (ECM) and modulate cellular processes by binding to cell surface receptors and initiating intracellular signal transduction. Their association with the ECM and the ability of some members of this protein family to regulate cell motility have opened up new avenues of research to investigate their functions in normal and diseased cells. In this review, we summarize the research on CyrA, an ECM calmodulin-binding protein in Dictyostelium. CyrA is proteolytically cleaved into smaller EGF-like (EGFL) repeat containing cleavage products during development. The first EGFL repeat of CyrA binds to the cell surface and activates a novel signalling pathway that modulates cell motility in this model organism. The similarity of CyrA to the most well-characterized matricellular proteins in mammals allows it to be designated as the first matricellular protein identified in Dictyostelium. 相似文献
8.
The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis 总被引:1,自引:1,他引:0
Elena Kypri Andri Christodoulou Giannis Maimaris Mette Lethan Maria Markaki Costas Lysandrou Carsten W. Lederer Nektarios Tavernarakis Stefan Geimer Lotte B. Pedersen Niovi Santama 《Cellular and molecular life sciences : CMLS》2014,71(3):517-538
Nucleotide-binding proteins Nubp1 and Nubp2 are MRP/MinD-type P-loop NTPases with sequence similarity to bacterial division site-determining proteins and are conserved, essential proteins throughout the Eukaryotes. They have been implicated, together with their interacting minus-end directed motor protein KIFC5A, in the regulation of centriole duplication in mammalian cells. Here we show that Nubp1 and Nubp2 are integral components of centrioles throughout the cell cycle, recruited independently of KIFC5A. We further demonstrate their localization at the basal body of the primary cilium in quiescent vertebrate cells or invertebrate sensory cilia, as well as in the motile cilia of mouse cells and in the flagella of Chlamydomonas. RNAi-mediated silencing of nubp-1 in C. elegans causes the formation of morphologically aberrant and additional cilia in sensory neurons. Correspondingly, downregulation of Nubp1 or Nubp2 in mouse quiescent NIH 3T3 cells markedly increases the number of ciliated cells, while knockdown of KIFC5A dramatically reduces ciliogenesis. Simultaneous double silencing of Nubp1 + KIFC5A restores the percentage of ciliated cells to control levels. We document the normal ciliary recruitment, during these silencing regimes, of basal body proteins critical for ciliogenesis, namely CP110, CEP290, cenexin, Chibby, AurA, Rab8, and BBS7. Interestingly, we uncover novel interactions of Nubp1 with several members of the CCT/TRiC molecular chaperone complex, which we find enriched at the basal body and recruited independently of the Nubps or KIFC5A. Our combined results for Nubp1, Nubp2, and KIFC5A and their striking effects on cilium formation suggest a central regulatory role for these proteins, likely involving CCT/TRiC chaperone activity, in ciliogenesis. 相似文献
9.
Inositol pyrophosphates: structure, enzymology and function 总被引:2,自引:0,他引:2
Christopher John Barker Christopher Illies Gian Carlo Gaboardi Per-Olof Berggren 《Cellular and molecular life sciences : CMLS》2009,66(24):3851-3871
The stereochemistry of the inositol backbone provides a platform on which to generate a vast array of distinct molecular motifs that are used to convey information both in signal transduction and many other critical areas of cell biology. Diphosphoinositol phosphates, or inositol pyrophosphates, are the most recently characterized members of the inositide family. They represent a new frontier with both novel targets within the cell and novel modes of action. This includes the proposed pyrophosphorylation of a unique subset of proteins. We review recent insights into the structures of these molecules and the properties of the enzymes which regulate their concentration. These enzymes also act independently of their catalytic activity via protein–protein interactions. This unique combination of enzymes and products has an important role in diverse cellular processes including vesicle trafficking, endo- and exocytosis, apoptosis, telomere length regulation, chromatin hyperrecombination, the response to osmotic stress, and elements of nucleolar function. 相似文献
10.
Alexander Y. Tsygankov 《Cellular and molecular life sciences : CMLS》2009,66(17):2949-2952
Two members of the TULA family (TULA/STS-2/UBASH3A and TULA-2/STS-1/UBASH3B) recently emerged as novel regulators of several
cellular functions. The degree of structural similarity between the TULA-family proteins is typical for proteins that belong
to the same family. Furthermore, the experiments with knockout mice lacking these proteins may be interpreted as suggesting
that functions of TULA-family proteins in T lymphocytes overlap. At the same time, TULA and TULA-2 exhibit clear functional
dissimilarities, starting with the finding that a conserved phosphatase domain present in both proteins exhibits remarkable
differences in enzymatic activity; TULA-2 is an active phosphatase capable of dephosphorylating multiple tyrosine-phosphorylated
proteins, whereas the phosphatase activity of TULA is extremely low. In contrast, TULA, but not TULA-2, facilitates growth
factor withdrawal-induced apoptosis in T cells. In spite of their apparent importance, the functional role of TULA-family
proteins is not well understood. In particular, the role of functional dissimilarities between them remains unclear. 相似文献
11.
Levy-Favatier F Leroux A Antoine B Nedelec B Delpech M 《Cellular and molecular life sciences : CMLS》2004,61(22):2886-2892
In a previous study, we identified and purified a 99-amino-acid rat liver-kidney perchloric-acid-soluble 23-kDa protein (P23) which displays 30% identity with a highly conserved domain of heat shock proteins (HSPs), as well as an AT-rich 3 untranslated region, which has also been described to play a role in H70 mRNA life span and protein expression. An identical perchloric-acid-soluble protein inhibiting protein synthesis in a rabbit reticulocyte lysate system was also found 2 years later by another group. More recently, the novel, the YjgF, protein family has been described, comprising, 24 full-length homologues, including P23, highly conserved through evolution, and consisting of approximately 130 residues each and sharing a common ternary structure. Independent studies from different laboratories have provided various hypothetical functions for each of these proteins. The high degree of evolutionary conservation may suggest that these proteins play an important role in cellular regulation. Although the function of none of these proteins is known precisely, we present experimental evidence which, combined with the relationship to glucose-regulating protein revealed here, and the relationship to fatty-acid-binding protein revealed by others, allow us to propose a role for P23. In rat liver, P23 expression is developmentally regulated and modulated by dietary glucose, and its mRNA is induced by starvation, in the presence of fatty-acids and in 3-MeDAB-induced hepatomas. The mRNA encoding mouse liver P23 is also hormonally modulated in a mouse line AT1F8. These data indicate that P23 protein might be a key controller of intermediary metabolism during fasting.Received 7 June 2003; received after revision 8 September 2004; accepted 10 October 2004 相似文献
12.
OSBP (oxysterol-binding protein) and ORPs (OSBP-related proteins) constitute an enigmatic eukaryotic protein family that is
united by a signature domain that binds oxysterols, sterols, and possibly other hydrophobic ligands. The human genome contains
12 OSBP/ORP family members genes, while that of the budding yeast Saccharomyces cerevisiae encodes seven OSBP homologues (Osh). Of these, Osh4 (also referred to as Kes1) has been the most widely studied to date.
Recently, three-dimensional crystal structures of Osh4 with and without sterols bound within the core of the protein were
determined. The core consists of 19 anti-parallel β-sheets that form a near-complete β-barrel. Recent work has suggested that
Osh proteins facilitate the non-vesicular transport of sterols in vivo and in vitro, while other evidence supports a role for Osh proteins in the regulation of vesicular transport and lipid metabolism.This
article will review recent advances in the study of ORP/Osh proteins and will discuss future research issues regarding the
ORP/Osh family.
Received 17 July 2007; received after revision 14 August 2007; accepted 12 September 2007 相似文献
13.
The Rh (Rhesus) genes encode a family of conserved proteins that share a structural fold of 12 transmembrane helices with
members of the major facilitator superfamily. Interest in this family has arisen from the discovery of Rh factor’s involvement
in hemolytic disease in the fetus and newborn, and of its homologs widely expressed in epithelial tissues. The Rh factor and
Rh-associated glycoprotein (RhAG), with epithelial cousins RhBG and RhCG, form four subgroups conferring upon vertebrates
a genealogical commonality. The past decade has heralded significant advances in understanding the phylogenetics, allelic
diversity, crystal structure, and biological function of Rh proteins. This review describes recent progress on this family
and the molecular insights gleaned from its gene evolution, membrane biology, and disease association. The focus is on its
long evolutionary history and surprising structural conservation from prokaryotes to humans, pointing to the importance of
its functional role, related to but distinct from ammonium transport proteins. 相似文献
14.
15.
R. T. Allen M. W. Cluck D. K. Agrawal 《Cellular and molecular life sciences : CMLS》1998,54(5):427-445
Apoptosis is an essential and highly conserved mode of cell death that is important for normal development, host defense
and suppression of oncogenesis. Faulty regulation of apoptosis has been implicated in degenerative conditions, vascular diseases,
AIDS and cancer. Among the numerous proteins and genes involved, members of the Bcl-2 family play a central role to inhibit
or promote apoptosis. In this article, we present up-to-date information and recent discoveries regarding biochemical functions
of Bcl-2 family proteins, positive and negative interactions between these proteins, and their modification and regulation
by either proteolytic cleavage or by cytosolic kinases, such as Raf-1 and stress-activated protein kinases. We have critically
reviewed the functional role of caspases and the consequences of cleaving key substrates, including lamins, poly(ADP ribose)
polymerase and the Rb protein. In addition, we have presented the latest Fas-induced signalling mechanism as a model for receptor-linked
caspase regulation. Finally, the structural and functional interactions of Ced-4 and its partial mam malian homologue, apoptosis
protease activating factor-1 (Apaf-1), are presented in a model which includes other Apafs. This model culminates in a caspase/Apaf
regulatory cascade to activate the executioners of programmed cell death following cytochrome c release from the mitochondria
of mammalian cells. The importance of these pathways in the treatment of disease is highly dependent on further characterization
of genes and other regulatory molecules in mammals.
Received 18 February 1998; accepted February 1998 相似文献
16.
T. Jenuwein G. Laible R. Dorn G. Reuter 《Cellular and molecular life sciences : CMLS》1998,54(1):80-93
The SET domain is a 130-amino acid, evolutionarily conserved sequence motif present in chromosomal proteins that function
in modulating gene activities from yeast to mammals. Initially identified as members of the Polycomb- and trithorax-group (Pc-G and trx-G) gene families, which are required to maintain expression boundaries of homeotic selector (HOM-C) genes,
SET domain proteins are also involved in position-effect-variegation (PEV), telomeric and centromeric gene silencing, and
possibly in determining chromosome architecture. These observations implicate SET domain proteins as multifunctional chromatin
regulators with activities in both eu- and heterochromatin – a role consistent with their modular structure, which combines
the SET domain with additional sequence motifs of either a cysteine-rich region/zinc-finger type or the chromo domain. Multiple
functions for chromatin regulators are not restricted to the SET protein family, since many trx-G (but only very few Pc-G)
genes are also modifiers of PEV. Together, these data establish a model in which the modulation of chromatin domains is mechanistically
linked with the regulation of key developmental loci (e.g. HOM-C). 相似文献
17.
Sangeeta Chauhan Xinde Zheng Yue Ying Tan Boon-Hui Tay Shuhui Lim Byrappa Venkatesh Philipp Kaldis 《Cellular and molecular life sciences : CMLS》2012,69(22):3835-3850
Successful completion of the cell cycle relies on the precise activation and inactivation of cyclin-dependent kinases (Cdks) whose activity is mainly regulated by binding to cyclins. Recently, a new family of Cdk regulators termed Speedy/RINGO has been discovered, which can bind and activate Cdks but shares no apparent amino acid sequence homology with cyclins. All Speedy proteins share a conserved domain of approximately 140 amino acids called “Speedy Box”, which is essential for Cdk binding. Speedy/RINGO proteins display an important role in oocyte maturation in Xenopus. Interestingly, a common feature of all Speedy genes is their predominant expression in testis suggesting that meiotic functions may be the most important physiological feature of Speedy genes. Speedy homologs have been reported in mammals and can be traced back to the most primitive clade of chordates (Ciona intestinalis). Here, we investigated the evolution of the Speedy genes and have identified a number of new Speedy/RINGO proteins. Through extensive analysis of numerous species, we discovered diverse evolutionary histories: the number of Speedy genes varies considerably among species, with evidence of substantial gains and losses. Despite the interspecies variation, Speedy is conserved among most species examined. Our results provide a complete picture of the Speedy gene family and its evolution. 相似文献
18.
Serine proteases exist in eukaryotic and prokaryotic organisms and have emerged during evolution as the most abundant and functionally diverse group. In Gram-negative bacteria, there is a growing family of high molecular weight serine proteases secreted to the external milieu by a fascinating and widely employed bacterial secretion mechanism, known as the autotransporter pathway. They were initially found in Neisseria, Shigella, and pathogenic Escherichia coli, but have now also been identified in Citrobacter rodentium, Salmonella, and Edwardsiella species. Here, we focus on proteins belonging to the serine protease autotransporter of Enterobacteriaceae (SPATEs) family. Recent findings regarding the predilection of serine proteases to host intracellular or extracellular protein-substrates involved in numerous biological functions, such as those implicated in cytoskeleton stability, autophagy or innate and adaptive immunity, have helped provide a better understanding of SPATEs’ contributions in pathogenesis. Here, we discuss their classification, substrate specificity, and potential roles in pathogenesis. 相似文献
19.
Teemu Haikarainen Anastassios C. Papageorgiou 《Cellular and molecular life sciences : CMLS》2010,67(3):341-351
Dps-like proteins are key factors involved in the protection of prokaryotic cells from oxidative damage. They act by either
oxidizing iron to prevent the formation of oxidative radicals or by forming Dps-DNA complexes to physically protect DNA. All
Dps-like proteins are characterized by a common three-dimensional architecture and are found as spherical dodecamers with
a hollow central cavity. Despite their structural similarities, recent biochemical and structural data have suggested different
functions among members of the family that range from protection inside the cells in response to various stress signals to
adhesion and virulence during bacterial infections. Moreover, the Dps-like proteins have lately attracted considerable interest
in the field of nanotechnology owing to their ability to act as protein cages for iron and various other metals. A better
understanding of their function and mechanism could therefore lead to novel applications in biotechnology and nanotechnology. 相似文献
20.
HERC proteins are defined as containing both HECT and RCC1-like domains in their amino acid sequences. Six HERC genes have turned up in the human genome which encode two different sorts of polypeptides: while the small HERC proteins possess little more than the two aforementioned domains, the large ones are giant proteins with a plethora of potentially important regions. It is now almost 10 years since the discovery of the first family member and information is starting to accumulate pointing to a general role for these proteins as ubiquitin ligases involved in membrane-trafficking events. In this review, the available data on these six members are discussed, together with an account of their evolution.Received 16 March 2005; received after revision 13 April 2005; accepted 28 April 2005 相似文献