CST Guide:

Section I: Research Areas
chapter 01: GENE EXPRESSION, EPIGENETICS, AND NUCLEAR FUNCTION
UV treatment
results in clustering
of cytosolic stress
granules containing
the translation repressor
protein TIAR.
Local Translation
Some mRNAs are transported in messenger ribonucleoprotein (mRNP) granules to their subcellular
locations and translated on-site in response to localized signals, known as local translation. This often
occurs during development, where protein gradients and varying expression patterns are necessary for
cellular differentiation. mRNPs include stress granules that store mRNA bound to stalled preinitiation
complexes and the translational repressors TIA-1 and TIAR until translational initiation can begin again
or the mRNA is degraded. In addition, mRNPs also include cytoplasmic processing bodies (P-bodies)
that function in mRNA turnover. Together, these elements can control translation, mRNA storage, and
stability in localized sites.
EDC4/Ge-1 is an essential component
of cytoplasmic P-bodies responsible
for mRNA decapping and degradation.
EDC4/Ge-1 Antibody #2548: Confocal IF analysis of HeLa cells using
#2548 (green). Actin filaments were labeled with DY-554 phalloidin (red).
Blue pseudocolor= DRAQ5 ® #4084 (fluorescent DNA dye).
Small noncoding RNAs
Small noncoding RNAs are important regulators of gene expression in higher eukaryotes. Several
classes of small RNAs, including short interfering RNAs (siRNAs), microRNAs (miRNAs), and Piwiinteracting
RNAs (piRNAs), have been identified. siRNAs are short segments (20–25 base pairs) of
double stranded RNA that silence expression of a single gene through complementary base pairing
that prevents target translation and/or promotes instability. siRNAs are commonly used in the research
community for antibody validation testing or gene silencing studies.
Similarly, microRNAs are about 21 nucleotides in length and have been implicated in many cellular
processes such as development, differentiation, and stress response. miRNAs function together with the
protein components of complexes called micro-ribonucleoproteins (miRNPs). Among the most important
components in these complexes are argonaute proteins. Argonaute proteins participate in the various
steps of microRNA-mediated gene silencing, such as repression of translation and mRNA turnover.
Silencing of DDX5 expression using DDX5 siRNA.
SignalSilence ® DDX5 siRNA I #8626 and SignalSilence ® DDX5 siRNA II #8627: WB analysis
of extracts from HeLa cells, transfected with 100 nM SignalSilence ® Control siRNA (Unconjugated)
#6568 (-), #8626 (+), or #8627 (+), using DDX5 (D15E10) XP ® Rabbit mAb #9877 (upper) or β-Actin
(13E5) Rabbit mAb #4970 (lower). The DDX5 (D15E10) XP ® Rabbit mAb confirms silencing of DDX5
expression, while the β-Actin (13E5) Rabbit mAb is used as a loading control.
Mili binds to piwi-interacting RNA in male germ
cells and is essential for spermatogenesis in mouse.
Mili (D14F5) XP ® Rabbit mAb #5940: Confocal IF analysis of mouse testis using #5940 (green) and
Pan-Keratin (C11) Mouse mAb #4545 (red). Blue pseudocolor = DRAQ5 ® #4084 (fluorescent DNA dye).
TIAR (D32D3) XP ® Rabbit mAb #8509:
Confocal IF analysis of HeLa cells, untreated
(left) or UV-treated (right), using #8509
(green). Actin filaments were labeled with
DY-554 phalloidin (red). Blue pseudocolor =
DRAQ5 ® #4084 (fluorescent DNA dye).
kDa
200
140
100
80
60
50
40
30
60
50
– +
I
II
+
DDX5
β-actin
DDX5 siRNA
Select Reviews
Adjibade, P. and Mazroui, R. (2014) Semin. Cell Dev. Biol. 34, 15–23. • Bar-Peled, L. and Sabatini, D.M. (2014) Trends Cell
Biol. 24, 400−406. • Donnelly, N., Gorman, A.M., Gupta, S., et al. (2013) Cell Mol. Life Sci. 70, 3493−3511. • Emde, A.
and Hornstein, E. (2014) EMBO J. 33,1428−1437. • Fabian, M.R., Payette, J., Holcik, M., et al. (2012) Nature 486, 126−129.
• Hershey, J.W., Sonenberg, N., and Mathews, M.B. (2012) Cold Spring Harb. Perspect. Biol. 4, a011528. • Hinnebusch, A.G.
and Lorsch, J.R. (2012) Cold Spring Harb. Perspect. Biol. 4, a011544. • Jung, H., Gkogkas, C.G., Sonenberg, N. et al. (2014)
Cell 157, 26−40. • Kong, J. and Lasko, P. (2012) Nat. Rev. Genet. 13, 383−394. • Spilka, R., Ernst, C., Mehta, A.K., et al.
(2013) Cancer Lett. 340, 9−21. • Thoreen, C.C. (2013) Biochem. Soc. Trans. 41, 913−916.
Commonly Studied Translational Control Targets
Target M P Target M P
4E-BP1
• • eIF4A
• •
Phospho-4E-BP1 • • eIF4B
• • PABP1
(Thr37/Thr46)
Phospho-eIF4B (Ser406) • •
Non-phospho-4E-BP1 • Phospho-eIF4B (Ser422) •
(Thr46)
eIF4E
• • PABP2
Phospho-4E-BP1 (Ser65) • •
Phospho-eIF4E (Ser209) • PACT
Phospho-4E-BP1 (Thr70) • •
eIF4G
• • Paip2A
4E-BP2
•
Phospho-eIF4G (Ser1108) • PARN
4EHP
•
eIF4GI
• • PERK
4E-T
•
eIF4G2/p97 • PKR
ADAR1
• •
EIF4H
• • PPIG
Argonaute 1 • •
eIF5
•
Argonaute 2 •
eIF6
• • PRP4K
Argonaute 3 •
ELAVL1/HuR • PTBP1
Argonaute 4 •
Exportin 5 • • Pumilio 1
BRF1/2
•
FMRP
• • Pumilio 2
CLK3
•
FUS/TLS
• RMP
CNOT2
•
FXR1
• • RPL11
CNOT3
•
FXR2
• •
CNOT6
•
GCN2
•
Coilin
•
hnRNP A0 • •
CPEB1
•
hnRNP A1 • •
DCP1B
•
hnRNP C1/C2 •
DDX3
• •
AUF1/hnRNP D •
DDX4
• •
hnRNP E1
•
DDX5
• •
hnRNP LL
•
DDX6/RCK • •
hnRNP K • •
DGCR8
•
SAM68
hnRNP Q/R • •
DHX29
• •
SF2/ASF
IMP1
• •
Dicer1
• •
SF3B1
IWS1
•
Drosha
•
SKAR
KHSRP
• •
EDC4/Ge-1
•
SKAR α/β
La Antigen • •
eEF1A
• •
SMN1
LSm2
•
eEF2
•
Symplekin
LysRS
• •
Phospho-eEF2 (Thr56) •
TFEB
MAPBPIP/ROBLD3/p14 •
eEF2k
•
THEX1
MAPKSP1/MP1 •
Phospho-eEF2k (Ser366) •
MetAP2 •
eIF1
•
TIAR
Mili
• •
eIF2α
• •
U2AF1
Miwi
• •
Phospho-eIF2α (Ser51) • •
Upf1
Mnk1
•
eIF2B-ε
•
Upf2
Phospho-Mnk1 •
eIF3A
• •
XBP-1s
(Thr197/202)
eIF3C
•
XRN2
MRPL11 • •
eIF3H
•
ZPR1
NCBP1/CBP80 •
eIF3J
• • NRF1/TCF11 •
eIF4A1
• NRF2
•
Target M P
NXF1
Asymmetric-Methyl-PABP1
(Arg455/Arg460)
Phospho-PPIG (Ser376)
S6 Ribosomal Protein
Phospho-S6 Ribosomal
Protein (Ser235/Ser236)
Phospho-S6 Ribosomal
Protein (Ser240/Ser244)
Ribosomal Protein L7a
Ribosomal Protein L13a
Ribosomal Protein L26
Ribosomal Protein S3
THOC4/ALY
•
•
•
•
•
•
•
•
•
•
•
•
•
•
•
•
•
• •
• •
•
•
• •
• •
•
•
•
•
• •
•
•
•
• •
•
• •
•
• •
•
•
•
•
These protein targets represent key
nodes within translational control
signaling pathways and are commonly
studied in translational control research.
Primary antibodies, antibody conjugates,
and antibody sampler kits containing
these targets are available from CST.
Listing as of September 2014. See our
website for current product information.
M Monoclonal Antibody
P Polyclonal Antibody
207
2012–2014 citations
CST antibodies for Phospho-S6
Ribosomal Protein (Ser235/236)
have been cited over 207 times in
high-impact, peer-reviewed publications
from the global research community.
Select Citations:
Wong, C.C. et al. (2014) Inactivating
CUX1 mutations promote tumorigenesis.
Nat. Genet. 46, 33−38.
Kurachi, M. et al. (2014) The
transcription factor BATF operates as
an essential differentiation checkpoint
in early effector CD8+ T cells. Nat.
Immunol. 15, 373−383.
Mouw, J.K. et al. (2014) Tissue
mechanics modulate microRNAdependent
PTEN expression to
regulate malignant progression.
Nat. Med. 20, 360−367.
Agarwal, A. et al. (2014) Antagonism
of SET using OP449 enhances the
efficacy of tyrosine kinase inhibitors
and overcomes drug resistance in
myeloid leukemia. Clin. Cancer Res.
20, 2092−2103.
Koo, J. et al. (2014) Maintaining
glycogen synthase kinase-3 activity
is critical for mTOR kinase inhibitors
to inhibit cancer cell growth. Cancer
Res. 7, 2555−2568.
Fay, M.M. et al. (2014) Enhanced
Arginine Methylation of Programmed
Cell Death 4 Protein during Nutrient
Deprivation Promotes Tumor
Cell Viability. J. Biol. Chem. 289,
17541−17552.
34 For Research Use Only. Not For Use in Diagnostic Procedures. See pages 302 & 303 for Pathway Diagrams, Application, and Reactivity keys.
www.cellsignal.com/csttranslational
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