Role of C-Terminal Tail Region of Human MtnB Enzyme for Its Tetramer Stability

2015 ◽  
Vol 36 (11) ◽  
pp. 2757-2760
Author(s):  
Hee Jung Ha ◽  
Ji Young Lee ◽  
Wonchull Kang ◽  
Jin Kuk Yang
Keyword(s):  
Tail Region ◽  
Tetramer Stability

The Role of the Coelomic Fluid in the Movements of Earthworms

1950 ◽  
Vol 27 (1) ◽  
pp. 110-122 ◽  
Author(s):  
G. E. NEWELL
Keyword(s):  
Short Review ◽  
The Body ◽  
Coelomic Fluid ◽  
Average Pressure ◽  
Normal Range ◽  
Tail Region ◽  
X Ray ◽  
Effective Barrier ◽  
Intrinsic Muscles

1. A short review is given of the coelom and of its morphological relations in the earthworm. 2. The arrangement of the intrinsic muscles in a typical septum is described. Four main sets of muscles are recognized: viz. radial muscles, circular muscles, oblique muscles, and the sphincter around the ventral foramen. 3. It is suggested that the function of the radial, circular and possibly of the oblique muscles is to control bulging of the septa, and so serve to localize differences in pressure in the coelomic fluid. Normally, in active worms, the sphincter of the ventral foramen is contracted and forms an effective barrier to the passage of fluid from one coelomic compartment to the next. This was verified experimentally and by X-ray photography. 4. A series of measurements of the pressure in the coelomic fluid in different regions of active worms was recorded by means of a capillary manometer and by the use of a spoon-gauge apparatus. Manometric measurements showed the average pressure in the anterior third of the body to be 16.0 cm. water and in the tail region to be 8.0 cm. water. The corresponding figures obtained with a spoon gauge were 13.5 and 8.5 cm. water. The pressure in narcotized worms is zero. 5. These results are discussed, and it is pointed out that the manometer readings suffer from the disadvantage of failing to show the rapid fluctuations in pressure which occur during wriggling movements of the worms. 6. It is calculated from these pressure readings that a worm can exert a forward thrust equivalent to forces of between 1.5 and 8.0 g. These figures agree well with those obtained by Gray & Lissman by the use of a special torsion balance. 7. The burrowing movements of earthworms are briefly described. 8. It is shown that the sphincters of the dorsal pores and of the nephridiopores do not normally allow of the escape of coelomic fluid, and will withstand a pressure well outside the normal range.

scholarly journals Neuroblast pattern and identity in the Drosophila tail region and role of doublesex in the survival of sex-specific precursors

Development ◽  
2013 ◽  
Vol 140 (8) ◽  
pp. 1830-1842 ◽  
Author(s):  
O. Birkholz ◽  
C. Rickert ◽  
C. Berger ◽  
R. Urbach ◽  
G. M. Technau
Keyword(s):  
Tail Region

scholarly journals Effect of Cytoplasmic Tail Truncations on the Activity of the M2 Ion Channel of Influenza A Virus

1999 ◽  
Vol 73 (12) ◽  
pp. 9695-9701 ◽  
Author(s):  
Kurt Tobler ◽  
Marie L. Kelly ◽  
Lawrence H. Pinto ◽  
Robert A. Lamb
Keyword(s):  
Ion Channel ◽  
Influenza A Virus ◽  
Influenza A ◽  
Transmembrane Domain ◽  
Stop Codon ◽  
Specific Inhibitor ◽  
Cytoplasmic Tail ◽  
Proton Channel ◽  
Tail Region

ABSTRACT The M2 protein of influenza A virus forms a proton channel that is required for viral replication. The M2 ion channel is a homotetramer and has a 24-residue N-terminal extracellular domain, a 19-residue transmembrane domain, and a 54-residue cytoplasmic tail. We show here that the N-terminal methionine residue is cleaved from the mature protein. Translational stop codons were introduced into the M2 cDNA at residues 46, 52, 62, 72, 77, 82, 87, and 92. The deletion mutants were designated truncx, according to the amino acid position that was changed to a stop codon. We studied the role of the cytoplasmic tail by measuring the ion channel activity (the current sensitive to the M2-specific inhibitor amantadine) of the cytoplasmic tail truncation mutants expressed in oocytes of Xenopus laevis. When their conductance was measured over time, mutants trunc72, trunc77, and trunc92 behaved comparably to wild-type M2 protein (a decrease of only 4% over 30 min). In contrast, conductance decreased by 28% for trunc82, 27% for trunc62, and 81% for trunc52 channels. Complete closure of the channel could be observed in some cells for trunc62 and trunc52 within 30 min. These data suggest that a role of the cytoplasmic tail region of the M2 ion channel is to stabilize the pore against premature closure while the ectodomain is exposed to low pH.

FGFR3 Associates with and Tyrosine-Phosphorylates p90RSK2, Leading to RSK2 Activation That Mediates Hematopoietic Transformation

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 3722-3722
Author(s):  
Sumin Kang ◽  
Shannon Elf ◽  
Shaozhong Dong ◽  
Taro Hitosugi ◽  
Ailan Guo ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Tyrosine Kinases ◽  
Mapk Pathway ◽  
Critical Role ◽  
Ectopic Expression ◽  
Alpha Helix ◽  
Tail Region ◽  
Murine Bone Marrow

Abstract Dysregulation of receptor tyrosine kinase FGFR3 has been implicated to play a pathogenic role in a number of human hematopoietic malignancies and solid tumors. These include t(4;14) multiple myeloma associated with ectopic expression of FGFR3 and t(4;12)(p16;p13) acute myeloid leukemia associated with expression of a constitutively activated fusion tyrosine kinase TEL-FGFR3. We recently reported that FGFR3 directly tyrosine phosphorylates p90 Ribosomal S6 Kinase2(RSK2) at Y529, which consequently regulates RSK2 activation [Kang et al, Cancer Cell 2007 Sep;12(3):201–14]. Here we identified Y707 as an additional tyrosine site of RSK2 that is phosphorylated by FGFR3. Phosphorylation at Y707 contributes to RSK2 activation, through a putative disruption of the autoinhibitory αL-helix on the C-terminus of RSK2, unlike Y529 phosphorylation that facilitates ERK binding. To elucidate the role of tyrosine phosphorylation at Y707 induced by FGFR3 in RSK2 activation, we characterized the RSK2 mutants with single Y→A and Y→F substitutions at Y707. RSK2 Y707F demonstrated decreased kinase activity, suggesting substitution of Y707 attenuates activation of RSK2 induced by FGFR3. Tyrosine phosphorylation at Y529 by FGFR3 regulates RSK2 activation by facilitating inactive ERK binding, whereas substitution of Y707 in RSK2 does not similarly attenuate inactive ERK binding to RSK2. Phosphorylation at Y707 may regulate RSK2 activation by affecting the structure of the autoinhibitory C-terminal domain of RSK2 since the Y707 is localized at the C-terminal tail region which represents a conserved putative auto-inhibitory alpha helix. Since other tyrosine kinases including FGFR1 and Src also phosphorylate RSK2 at Y529 and Y707, tyrosine phosphorylation may be a general requirement for RSK2 activation through the ERK/MAPK pathway. Together, our current and previous findings represent a paradigm for tyrosine phosphorylation-dependent regulation of serine-threonine kinases. Moreover, we found that FGFR3 interacts with RSK2 through residue W332 in the linker region of RSK2, and that this association is required for FGFR3-dependent phosphorylation of RSK2 at Y529 and Y707, and subsequent RSK2 activation. Furthermore, in a murine bone marrow transplant assay, genetic deficiency in RSK2 resulted in a significantly delayed and attenuated myeloproliferative syndrome induced by TEL-FGFR3 as compared with wild type cells, suggesting a critical role of RSK2 in FGFR3-induced hematopoietic transformation.

The Possible Role of the Supra-Oesophageal Ganglion in the Responses of Nephtys (Polychaeta, Annelida) to Changes in Hydrostatic Pressure

1969 ◽  
Vol 51 (1) ◽  
pp. 171-179
Author(s):  
ELFED MORGAN
Keyword(s):  
Hydrostatic Pressure ◽  
The Body ◽  
Swimming Activity ◽  
Tail Region ◽  
Sensory Structures

1. The swimming activity of the isolated ‘tail’ region of Nephtys is not affected by changes in hydrostatic pressure. In contrast the responses shown by the isolated anterior third of the body are indistinguishable from those of intact worms. 2. Decerebration, or transection of both circum-oesophageal connectives, also destroys the worms' ability to respond, whereas transection of the connective on one side only does not. 3. Not one of the sensory structures hitherto described in association with the supra-oesophageal ganglion appears to be the sole mediator of the response.

The carboxy terminus of Tub4p is required for gamma-tubulin function in budding yeast

2000 ◽  
Vol 113 (21) ◽  
pp. 3871-3882 ◽  
Author(s):  
J. Vogel ◽  
M. Snyder
Keyword(s):  
Temperature Sensitive ◽  
Carboxy Terminus ◽  
Tail Region ◽  
Microtubule Organization ◽  
Electron Microscopic ◽  
Bud Neck ◽  
Cytoplasmic Microtubules ◽  
Gamma Tubulin ◽  
Carboxy Terminal

The role of gamma-tubulin in microtubule nucleation is well established, however, its function in other aspects of microtubule organization is unknown. The carboxy termini of alpha/beta-tubulins influence the assembly and stability of microtubules. We investigated the role of the carboxy terminus of yeast gamma-tubulin (Tub4p) in microtubule organization. This region consists of a conserved domain (DSYLD), and acidic tail. Cells expressing truncations lacking the DSYLD domain, tail or both regions are temperature sensitive for growth. Growth defects of tub4 mutants lacking either or both carboxy-terminal domains are suppressed by the microtubule destabilizing drug benomyl. tub4 carboxy-terminal mutants arrest as large budded cells with short bipolar spindles positioned at the bud neck. Electron microscopic analysis of wild-type and CTR mutant cells reveals that SPBs are tightly associated with the bud neck/cortex by cytoplasmic microtubules in mutants lacking the tail region (tub4-delta 444, tub4-delta 448). Mutants lacking the DSYLD residues (tub4-delta 444, tub4-delta DSYLD) form many cytoplasmic microtubules. We propose that the carboxy terminus of Tub4p is required for re-organization of the microtubules upon completion of nuclear migration, and facilitates spindle elongation into the bud.

scholarly journals The Role of the Cytoplasmic Tail Region of Influenza Virus Hemagglutinin in Formation and Growth of Fusion Pores

Virology ◽  
1997 ◽  
Vol 235 (1) ◽  
pp. 118-128 ◽  
Author(s):  
Grigory B. Melikyan ◽  
Hong Jin ◽  
Robert A. Lamb ◽  
Fredric S. Cohen
Keyword(s):  
Influenza Virus ◽  
Cytoplasmic Tail ◽  
Tail Region ◽  
Influenza Virus Hemagglutinin ◽  
Fusion Pores

Role of the C-Terminal Tail Region in the Self-Assembly of .lambda.-Repressor

Biochemistry ◽  
1995 ◽  
Vol 34 (15) ◽  
pp. 5090-5097 ◽  
Author(s):  
Sumita Bandyopadhyay ◽  
Utpal Banik ◽  
Bhabatarak Bhattacharyya ◽  
Nitai C. Mandal ◽  
Siddhartha Roy
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Tail Region ◽  
Lambda Repressor

scholarly journals Syntaxins 6 and 8 facilitate tau into secretory pathways

2021 ◽  
Author(s):  
Wei Siang Lee ◽  
Daniel CS Tan ◽  
Yuanyuan Deng ◽  
Annika van Hummel ◽  
Stefania Ippati ◽  
...  
Keyword(s):  
Progressive Supranuclear Palsy ◽  
Molecular Mechanisms ◽  
Transmembrane Domain ◽  
Brain Regions ◽  
Tau Pathology ◽  
Tail Region ◽  
Secretory Pathways ◽  
Donor Cells ◽  
Neuronal Connections

Tau pathology initiates in defined brain regions and is known to spread along neuronal connections as symptoms progress in Alzheimer’s disease (AD) and other tauopathies. This spread requires the release of tau from donor cells, but the underlying molecular mechanisms remained unknown. Here, we established the interactome of the C-terminal tail region of tau and identified syntaxin 8 (STX8) as a mediator of tau release from cells. Similarly, we showed the syntaxin 6 (STX6), part of the same SNARE family as STX8 also facilitated tau release. STX6 was previously genetically linked to progressive supranuclear palsy (PSP), a tauopathy. Finally, we demonstrated that the transmembrane domain of STX6 is required and sufficient to mediate tau secretion. The differential role of STX6 and STX8 in alternative secretory pathways suggests association of tau with different secretory processes. Taken together, both syntaxins, STX6 and STX8, may contribute to AD and PSP pathogenesis by mediating release of tau from cells and facilitating pathology spreading.

scholarly journals GMx33 Associates with the Trans-Golgi Matrix in a Dynamic Manner and Sorts within Tubules Exiting the Golgi

2006 ◽  
Vol 17 (1) ◽  
pp. 511-524 ◽  
Author(s):  
Christopher M. Snyder ◽  
Gonzalo A. Mardones ◽  
Mark S. Ladinsky ◽  
Kathryn E. Howell
Keyword(s):  
Live Cell Imaging ◽  
Cell Imaging ◽  
Matrix Proteins ◽  
Dependent Manner ◽  
Tail Region ◽  
Cytoplasmic Face ◽  
Golgi Structure ◽  
Golgi Matrix

The trans-Golgi matrix consists of a group of proteins dynamically associated with the trans-Golgi and thought to be involved in anterograde and retrograde Golgi traffic, as well as interactions with the cytoskeleton and maintenance of the Golgi structure. GMx33 is localized to the cytoplasmic face of the trans-Golgi and is also present in a large cytoplasmic pool. Here we demonstrate that GMx33 is dynamically associated with the trans-Golgi matrix, associating and dissociating with the Golgi in seconds. GMx33 can be locked onto the trans-Golgi matrix by GTPγS, indicating that its association is regulated in a GTP-dependent manner like several other Golgi matrix proteins. Using live-cell imaging we show that GMx33 exits the Golgi associated with tubules and within these tubules GMx33 segregates from transmembrane proteins followed by fragmentation of the tubules into smaller tubules and vesicles. Within vesicles produced by an in vitro budding reaction, GMx33 remains segregated in a matrixlike tail region that sometimes contains Golgin-245. This trans-matrix often links a few vesicles together. Together these data suggest that GMx33 is a member of the trans-Golgi matrix and offer clues regarding the role of the trans-Golgi matrix in sorting and exit from the Golgi.

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