Transduction of TAT Fusion Proteins into the Human and Bovine Trabecular Meshwork

2006 ◽  
Vol 47 (10) ◽  
pp. 4427-4434 ◽  
Author(s):  
H. Sakai
Keyword(s):  
Trabecular Meshwork ◽  
Fusion Proteins ◽  
Tat Fusion Proteins

scholarly journals Recognition of RNA Branch Point Sequences by the KH Domain of Splicing Factor 1 (Mammalian Branch Point Binding Protein) in a Splicing Factor Complex

2001 ◽  
Vol 21 (15) ◽  
pp. 5232-5241 ◽  
Author(s):  
Hadas Peled-Zehavi ◽  
J. Andrew Berglund ◽  
Michael Rosbash ◽  
Alan D. Frankel
Keyword(s):  
Branch Point ◽  
Fusion Proteins ◽  
Rna Binding ◽  
Binding Protein ◽  
Splicing Factor ◽  
Splice Sites ◽  
Reporter System ◽  
Kh Domain ◽  
Tat Fusion Proteins ◽  
Splicing Factor 1

ABSTRACT Mammalian splicing factor 1 (SF1; also mammalian branch point binding protein [mBBP]; hereafter SF1/mBBP) specifically recognizes the seven-nucleotide branch point sequence (BPS) located at 3′ splice sites and participates in the assembly of early spliceosomal complexes. SF1/mBBP utilizes a “maxi-K homology” (maxi-KH) domain for recognition of the single-stranded BPS and requires a cooperative interaction with splicing factor U2AF65 bound to an adjacent polypyrimidine tract (PPT) for high-affinity binding. To investigate how the KH domain of SF1/mBBP recognizes the BPS in conjunction with U2AF and possibly other proteins, we constructed a transcriptional reporter system utilizing human immunodeficiency virus type 1 Tat fusion proteins and examined the RNA-binding specificity of the complex using KH domain and RNA-binding site mutants. We first established that SF1/mBBP and U2AF cooperatively assemble in our reporter system at RNA sites composed of the BPS, PPT, and AG dinucleotide found at 3′ splice sites, with endogenous proteins assembled along with the Tat fusions. We next found that the activities of the Tat fusion proteins on different BPS variants correlated well with the known splicing efficiencies of the variants, supporting a model in which the SF1/mBBP-BPS interaction helps determine splicing efficiency prior to the U2 snRNP-BPS interaction. Finally, the likely RNA-binding surface of the maxi-KH domain was identified by mutagenesis and appears similar to that used by “simple” KH domains, involving residues from two putative α helices, a highly conserved loop, and parts of a β sheet. Using a homology model constructed from the cocrystal structure of a Nova KH domain-RNA complex (Lewis et al., Cell 100:323–332, 2000), we propose a plausible arrangement for SF1/mBBP-U2AF complexes assembled at 3′ splice sites.

scholarly journals Antitumour effects of PLC-γ1-(SH2)2-TAT fusion proteins on EGFR/c-erbB-2-positive breast cancer cells

2004 ◽  
Vol 90 (1) ◽  
pp. 230-235 ◽  
Author(s):  
Y Katterle ◽  
B H Brandt ◽  
S F Dowdy ◽  
B Niggemann ◽  
K S Zänker ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Fusion Proteins ◽  
Breast Cancer Cells ◽  
Tat Fusion Proteins ◽  
Antitumour Effects ◽  
Positive Breast Cancer

Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins

2004 ◽  
Vol 319 (1) ◽  
pp. 12-20 ◽  
Author(s):  
Nicolas J Caron ◽  
Simon P Quenneville ◽  
Jacques P Tremblay
Keyword(s):  
Fusion Proteins ◽  
Tat Fusion Proteins

scholarly journals Caveolae-Mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time

2003 ◽  
Vol 8 (2) ◽  
pp. 284-294 ◽  
Author(s):  
Aldo Ferrari ◽  
Vittorio Pellegrini ◽  
Caterina Arcangeli ◽  
Antonio Fittipaldi ◽  
Mauro Giacca ◽  
...  
Keyword(s):  
Real Time ◽  
Fusion Proteins ◽  
Tat Fusion Proteins ◽  
Hiv 1

scholarly journals Cell Membrane Lipid Rafts Mediate Caveolar Endocytosis of HIV-1 Tat Fusion Proteins

2003 ◽  
Vol 278 (36) ◽  
pp. 34141-34149 ◽  
Author(s):  
Antonio Fittipaldi ◽  
Aldo Ferrari ◽  
Monica Zoppé ◽  
Caterina Arcangeli ◽  
Vittorio Pellegrini ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Lipid Rafts ◽  
Fusion Proteins ◽  
Membrane Lipid ◽  
Tat Fusion Proteins ◽  
Hiv 1

Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration

10.1038/4042 ◽  
1998 ◽  
Vol 4 (12) ◽  
pp. 1449-1452 ◽  
Author(s):  
Hikaru Nagahara ◽  
Adamina M. Vocero-Akbani ◽  
Eric L. Snyder ◽  
Alan Ho ◽  
Dawn G. Latham ◽  
...  
Keyword(s):  
Cell Migration ◽  
Fusion Proteins ◽  
Mammalian Cells ◽  
Full Length ◽  
Tat Fusion Proteins
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