Smad oligomerisation. Smad oligomerisation. Pictorial representation of the plasma membrane receptor kinases that phosphorylate the C-termini of R-Smads.

Slides:



Advertisements
Similar presentations
Books Molecular Cell Biology Lodish
Advertisements

SIGNAL TRANSDUCTION Signal Transduction Pathway Protein Modification Phosphorylation Cascade Protein Kinases.
In vitro phosphorylation of condensin SMC requires the ATPase domain.
binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for binding. 50 of these correspond.
دکتر مجیری داروساز متخصص فارماکولوژی
Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus
A New Twist in Smad Signaling
Yvonne Groemping, Karine Lapouge, Stephen J. Smerdon, Katrin Rittinger 
Smads “Freeze” When They Ski
Volume 17, Issue 6, Pages (March 2005)
Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.
Cell Communication (Signaling) Part 3
Signaling Network Model of Chromatin
Flavivirus particle assembly
Cell Membranes: The Lipid Perspective
Volume 19, Issue 9, Pages (May 2017)
Volume 26, Issue 2, Pages e4 (February 2018)
Mark A. Lemmon, Daniel M. Freed, Joseph Schlessinger, Anatoly Kiyatkin 
TGFβ Signaling in Growth Control, Cancer, and Heritable Disorders
Signaling Takes Shape in the Immune System
Cell Communication (Signaling) Part 3
Fusion process between the RSV envelope and cellular membrane.
Stable interactors of Plk1 include phosphorylation-dependent interactions. Stable interactors of Plk1 include phosphorylation-dependent interactions. (A)
Non-Smad signalling. Non-Smad signalling. The canonical Smad pathway starting from the ligand-receptor complex and ending in the nucleus is illustrated.
(A) The canonical Smad pathway.
Fig. 2. Histone H3 phosphorylation appears at prometaphase upon C4 treatment.(A) Western blots were realized on cells synchronized at mitotic entry in.
IQGAP3 is a novel member of the IQGAP family.
Fig. 4. The model of malate metabolism in fruit cells under different K level conditions. The model of malate metabolism in fruit cells under different.
In Search of the Hair-Cell Gating Spring
(A) Deduced amino acid sequence of the D2SV cDNA cloned from the mouse heart RNA. The novel 20 amino acid C-terminus (CT) is underlined. (A) Deduced amino.
Fig. 2 Views of the Pincer-FATKIN interface and the dimer interface.
Fig. 2. Centrosomal proteins display distinct localizations and radial distances from centriole walls.U2OS cells were fixed and stained with the indicated.
Transcription factor network of human pancreas development.
HEAT repeats as part of large protein complexes.
The TGFβ large latent complex (LLC).
Src tethers Cas to adhesion complexes.
Homozygous col22a1−/− embryos show increased percentage of hemorrhages when raised at increased temperature. Homozygous col22a1−/− embryos show increased.
Example of a putative bridging fiber.
Fig. 1. Optogenetic activation of EphB2.
The AUX and PIN auxin carrier proteins are transported by both ESCRT-dependent and ESCRT-independent pathways. The AUX and PIN auxin carrier proteins are.
Functions of AP-1 subunits in various cellular processes and disease.
Regulation of lipid droplet formation by PI3-kinase activity.
The expression of two forms of N-cadherin.
HADAT1 is a nucleocytoplasmic shuttling protein that is excluded from the nucleolus. hADAT1 is a nucleocytoplasmic shuttling protein that is excluded from.
Marginal means (±s.e.m.) of temperatures for four tissues in 13 king penguins while fasting in water. Marginal means (±s.e.m.) of temperatures for four.
Signalling specificity in the TGF-β superfamily.
EB1 localization to the centrosome is mediated by its C-terminal domain. EB1 localization to the centrosome is mediated by its C-terminal domain. Sections.
Smad signalling centres.
Peroxisome speeds were slower in patient and control cells.
EB1 and its C-terminal binding partner APC co-purify with centrosomes.
Met-misincorporated residues in Flag-VN–AIMP3 and their location in the AIMP3 and Venus structures. Met-misincorporated residues in Flag-VN–AIMP3 and their.
Transcriptional regulation by Smads.
The BRCA1 aggregates exclude large nuclear structures.
Kinetics of BDNF-induced Erk, Akt and PLCγ activation in the presence of 15 mM NaCl or 15 mM KCl. Representative western blots (A) and quantitative plots.
Schematic diagram of the interactions between retromer and its associated proteins. Schematic diagram of the interactions between retromer and its associated.
The stenotele explosion process (modified from Tardent and Holstein, 1982). The stenotele explosion process (modified from Tardent and Holstein, 1982).
Mapping of the interaction domains in LMTK2 and myosin VI
Vps36 interacts with Smo in the absence of Hh
TRIM–SLR interactions and the TRIMosome.
Instances during the time course of wake generation behind a steadily swimming eel (speed U=0.121 m s-1, sequence 1, see Table 1). Instances during the.
Epiplakin binds to keratins via multiple sites.
The dynamics of Akt activation in cultured human keratinocytes.
DAPK interacts with HSF1 in vivo and in vitro.
Detection of phosphorylated Smad2/3 (pSmad2/3) in the skin of wild-type and transgenic animals during the first hair cycle. Detection of phosphorylated.
Phylogenetic analysis and domain structure of CALM proteins.
Susan S. Taylor, Nina M. Haste, Gourisankar Ghosh  Cell 
Volume 7, Issue 1, Pages 1-11 (July 1997)
Urea transport across an IMCD cell.
Rho and Rac Take Center Stage
Volume 19, Issue 9, Pages (May 2017)
Presentation transcript:

Smad oligomerisation. Smad oligomerisation. Pictorial representation of the plasma membrane receptor kinases that phosphorylate the C-termini of R-Smads (light colour), leading to homo-oligomerisation (a dimer shown for simplicity). Hetero-oligomerisation of R-Smads with the Co-Smad (dark colour) is shown leading to dimers and trimers (see text). The MH1 and MH2 domains are drawn and coloured according to the depiction of Table 1. Small black circles represent the di-phosphate modification of the SXS motif and small, double-headed arrows point to the protein interface between phosphorylated C-termini and the MH2 domain. For references see Chacko et al. (Chacko et al., 2001) and Shi (Shi, 2001). Aristidis Moustakas et al. J Cell Sci 2001;114:4359-4369 © The Company of Biologists Limited 2001