Disease relevance of FKSG30

• Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis [1].
• Increased expression of actin-like protein in human and ethylnitrosourea-induced tumors of the nervous system [2].
• The structure of the cytoplasmic domain of EpsL, an inner membrane component of the type II secretion system of Vibrio cholerae: an unusual member of the actin-like ATPase superfamily [3].
• Compared to the other specimen groups, biopsies of basal cell carcinomas reveal a decrease in hemidesmosomes and an increase in actin-like microfilaments in cells at the margins of the tumors [4].
• When examining proteins in human pigment tissues, we found that a third actin-like protein, in addition to beta- and gamma-actin was more frequent and in a larger amount in benign tissues such as blue nevus and nevus pigmentosus, than in malignant melanoma [5].

High impact information on FKSG30

• The distribution of the proteins in different species of bacteria, and the similarity of their sequence to eukaryotic actins, suggest that the MreB-like proteins have a cytoskeletal, actin-like role in bacterial cell morphogenesis [1].
• On the one hand, the determination of the structure of a bacterial actin-like protein MreB reveals the prokaryotic origins of the actin cytoskeleton, whereas on the other, cryo-electron microscopy and crystallography have yielded reconstructions of many actin crosslinking, regulatory and binding proteins in complex with F-actin [6].
• ParM, the actin-like ATPase of plasmid R1, forms dynamic filaments that segregate plasmids paired at mid-cell to daughter cells [7].
• By using fluorescently labeled phalloidin we have examined, at the light microscope level, the three-dimensional distribution and reorganization of actin-like microfilaments (mfs) during plant cell cycle and differentiation [8].
• The latter technique reveals that actin-like microfilaments are identifiable in spindles of glycerinated cells before and after addition of S-1 or HMM [9].

Chemical compound and disease context of FKSG30

• Actin-like contractile protein in carbon tetrachloride-induced cirrhosis in the rat [10].

Biological context of FKSG30

• Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles [11].
• This revealed a structural flexibility that has previously been described as a "butterfly-like" cleft opening around the active site in other actin-like superfamily proteins [12].
• The high-resolution crystal structure of the putative Aquifex aeolicus PPX/GPPA phosphatase from the actin-like ATPase domain superfamily has been determined, providing the first insights to features of the common catalytic core of the PPX/GPPA family [12].
• It is concluded that microfilaments in theca fibroblasts are actin-like and may contract to provide the mechanism of expulsion for the oocyte during ovulation [13].
• The presence of both actin-like and myosin-like proteins would be consistent with a role in gliding and other cell motility processes of this parasite [14].

Anatomical context of FKSG30

• It is suggested that cytoplasmic and perinuclear NGF may be be in contact with a pool of tubulin or actin-like proteins in their soluble or organized form and play a key role in the process of arrest of division and neurite growth [15].
• Treatment of the membranes of labeled cells in a low ionic strength alkaline medium did not alter radioactive peaks and demonstrated that Peak C differed from the actin-like membrane protein [16].
• It has been suggested that angiogenin binds to an actin-like molecule present on the surface of endothelial cells [17].
• It is suggested that actin-like filaments are localized in the region of the fibrous collar and in the epiplasm, and that these are involved in tentacle retraction; whilst the microtubules of the axoneme are concerned with feeding, and play only a cytoskeletal role in the contractile mechanism [18].
• An actin-like protein was purified to apparent homogeneity from chick-embryo homogenates and chick-embryo fibroblasts by the use of poly-L-proline-agarose affinity chromatography; we therefore refer to this protein as PBP (poly-L-proline-binding protein) [19].

Associations of FKSG30 with chemical compounds

• Peak C migrated like glycoprotein PAS-2 and protein Band 5, the actin-like, water-soluble membrane protein [16].
• Furthermore, the addition of a fluorescein-labeled anti-S100C (beta-actin binding protein) antibody mixed with PEI-protein G to human fibroblasts resulted in the appearance of a fluorescence image of actin-like filamentous structures in the cells [20].
• In this context, we have co-purified a human myometrial adenylate cyclase with an actin-like protein in a two-step purification protocol [21].
• Double labeling indirect immunofluorescence showed that Dp71f colocalized with actin-like beta-dystroglycan and beta-1 integrin [22].

Physical interactions of FKSG30

• We also report for the first time that alpha-actinin and filamin purified from chicken gizzard both interact with a prokaryotic actin-like protein [23].

Other interactions of FKSG30

• Two genetically closely related sequences, FKSG30 and an actin-like sequence in the Cat Eye syndrome region, were found to cluster with the kappa-actins [24].
• The actin-like protein, component 5, is identical with human uterine actin in its ability to form 50-70-A filaments to stimulate myosin ATPase activity, and to bind rabbit heavy meromyoson specit heavy meromyosin specifically [25].
• We propose that this third actin-like protein is probably smooth muscle alpha-actin and that different expressions of this third actin may possibly serve as a sensitive biochemical marker for the diagnosis of human malignant melanoma [5].

Analytical, diagnostic and therapeutic context of FKSG30

• Previous studies have identified an "actin-like" protein in human sperm by indirect immunofluorescence microscopy with various probes, but no real biochemical confirmation of actin was made [26].
• Identification of actin-like proteins in alcoholic hyaline by immunofluorescence [27].
• Further characterisation of this protein by two-dimensional gel electrophoresis suggested that it is an actin-like polypeptide [28].
• Actin and/or actin-like protein have been localized in the cellular and acellular components of the glomerular walls of mouse kidney by means of immunoelectron microscopy, employing human antibodies to smooth muscle (SMA) [29].
• When a planarian is induced to regenerate by head amputation, the immunostaining of the alpha-sm actin-like molecule becomes important in the area of growing blastema, reaching a maximum between 70-120 hours after injury [30].

References