scholarly journals Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy

Author(s):  
Ronny Peri-Naor ◽  
Leila Motiei ◽  
David Margulies
2009 ◽  
Vol 47 (05) ◽  
Author(s):  
G Kéri ◽  
L Őrfi ◽  
Z Greff ◽  
Z Varga ◽  
B Szokol ◽  
...  

Author(s):  
M. Madhumalini ◽  
T. Meera Devi

The article has been withdrawn on the request of the authors and the editor of the journal Current Signal Transduction Therapy. Bentham Science apologizes to the readers of the journal for any inconvenience this may have caused. BENTHAM SCIENCE DISCLAIMER: It is a condition of publication that manuscripts submitted to this journal have not been published and will not be simultaneously submitted or published elsewhere. Furthermore, any data, illustration, structure or table that has been published elsewhere must be reported, and copyright permission for reproduction must be obtained. Plagiarism is strictly forbidden, and by submitting the article for publication the authors agree that the publishers have the legal right to take appropriate action against the authors, if plagiarism or fabricated information is discovered. By submitting a manuscript the authors agree that the copyright of their article is transferred to the publishers, if and when the article is accepted for publication.


Membranes ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 222
Author(s):  
Agnieszka Polit ◽  
Paweł Mystek ◽  
Ewa Błasiak

In highly organized multicellular organisms such as humans, the functions of an individual cell are dependent on signal transduction through G protein-coupled receptors (GPCRs) and subsequently heterotrimeric G proteins. As most of the elements belonging to the signal transduction system are bound to lipid membranes, researchers are showing increasing interest in studying the accompanying protein–lipid interactions, which have been demonstrated to not only provide the environment but also regulate proper and efficient signal transduction. The mode of interaction between the cell membrane and G proteins is well known. Despite this, the recognition mechanisms at the molecular level and how the individual G protein-membrane attachment signals are interrelated in the process of the complex control of membrane targeting of G proteins remain unelucidated. This review focuses on the mechanisms by which mammalian Gα subunits of G proteins interact with lipids and the factors responsible for the specificity of membrane association. We summarize recent data on how these signaling proteins are precisely targeted to a specific site in the membrane region by introducing well-defined modifications as well as through the presence of polybasic regions within these proteins and interactions with other components of the heterocomplex.


2005 ◽  
Vol 79 (19) ◽  
pp. 12173-12184 ◽  
Author(s):  
Bok-Soo Lee ◽  
Sun-Hwa Lee ◽  
Pinghui Feng ◽  
Heesoon Chang ◽  
Nam-Hyuk Cho ◽  
...  

ABSTRACT Kaposi's sarcoma (KS) is a multifocal angiogenic tumor and appears to be a hyperplastic disorder caused, in part, by local production of inflammatory cytokines. The K1 lymphocyte receptor-like protein of KS-associated herpesvirus (KSHV) efficiently transduces extracellular signals to elicit cellular activation events through its cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM). To further delineate K1-mediated signal transduction, we purified K1 signaling complexes and identified its cellular components. Upon stimulation, the K1 ITAM was efficiently tyrosine phosphorylated and subsequently interacted with cellular Src homology 2 (SH2)-containing signaling proteins Lyn, Syk, p85, PLCγ2, RasGAP, Vav, SH2 domain-containing protein tyrosine phosphatase 1/2, and Grab2 through its phosphorylated tyrosine residues. Mutational analysis demonstrated that each tyrosine residue of K1 ITAM contributed to the interactions with cellular signaling proteins in distinctive ways. Consequently, these interactions led to the marked augmentation of cellular signal transduction activity, evidenced by the increase of cellular tyrosine phosphorylation and intracellular calcium mobilization, the activation of NF-AT and AP-1 transcription factor activities, and the production of inflammatory cytokines. These results demonstrate that KSHV K1 effectively recruits a set of cellular SH2-containing signaling molecules to form the K1 signalosome, which elicits downstream signal transduction and induces inflammatory cytokine production.


2007 ◽  
Vol 2 (1) ◽  
pp. 91-100
Author(s):  
Sho-ichi Yamagishi ◽  
Kazuo Nakamura ◽  
Takanori Matsui ◽  
Yumiko Yoshida ◽  
Katsuhiko Takenaka ◽  
...  

Author(s):  
Hari Krishnan P

The article has been withdrawn at the request of the authors and editor of the journal Current Signal Transduction Therapy Bentham Science apologizes to the readers of the journal for any inconvenience this may have caused. The Bentham Editorial Policy on Article Withdrawal can be found at https://benthamscience.com/editorial-policies-main.php BENTHAM SCIENCE DISCLAIMER: It is a condition of publication that manuscripts submitted to this journal have not been published and will not be simultaneously submitted or published elsewhere. Furthermore, any data, illustration, structure or table that has been published elsewhere must be reported, and copyright permission for reproduction must be obtained. Plagiarism is strictly forbidden, and by submitting the article for publication the authors agree that the publishers have the legal right to take appropriate action against the authors, if plagiarism or fabricated information is discovered. By submitting a manuscript, the authors agree that the copyright of their article is transferred to the publishers if and when the article is accepted for publication.


2006 ◽  
Vol 1 (1) ◽  
pp. 67-95 ◽  
Author(s):  
Gyorgy Keri ◽  
Laszlo Orfi ◽  
Daniel Eros ◽  
Balint Hegymegi-Barakonyi ◽  
Csaba Szantai-Kis ◽  
...  

2000 ◽  
Vol 151 (2) ◽  
pp. 199-208 ◽  
Author(s):  
Thomas Harder ◽  
Marina Kuhn

Activation of T cell antigen receptor (TCR) induces tyrosine phosphorylations that mediate the assembly of signaling protein complexes. Moreover, cholesterol-sphingolipid raft membrane domains have been implicated to play a role in TCR signal transduction. Here, we studied the assembly of TCR with signal transduction proteins and raft markers in plasma membrane subdomains of Jurkat T leukemic cells. We employed a novel method to immunoisolate plasma membrane subfragments that were highly concentrated in activated TCR–CD3 complexes and associated signaling proteins. We found that the raft transmembrane protein linker for activation of T cells (LAT), but not a palmitoylation-deficient non-raft LAT mutant, strongly accumulated in TCR-enriched immunoisolates in a tyrosine phosphorylation–dependent manner. In contrast, other raft-associated molecules, including protein tyrosine kinases Lck and Fyn, GM1, and cholesterol, were not highly concentrated in TCR-enriched plasma membrane immunoisolates. Many downstream signaling proteins coisolated with the TCR/LAT-enriched plasma membrane fragments, suggesting that LAT/TCR assemblies form a structural scaffold for TCR signal transduction proteins. Our results indicate that TCR signaling assemblies in plasma membrane subdomains, rather than generally concentrating raft-associated membrane proteins and lipids, form by a selective protein-mediated anchoring of the raft membrane protein LAT in vicinity of TCR.


2007 ◽  
Vol 2 (1) ◽  
pp. 21-30 ◽  
Author(s):  
Syed Hussain ◽  
Daniel Rea ◽  
Nicholas James ◽  
Daniel Palmer

2015 ◽  
Vol 7 (16) ◽  
pp. 2091-2093 ◽  
Author(s):  
Ronny Peri-Naor ◽  
Leila Motiei ◽  
David Margulies

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