Febs Letters

doi: 10.1016/S0014-5793(11)00422-4pmid: N/A

Yoshida, Hitomi; Kitagishi, Yasuko; Okumura, Naoko; Murakami, Mutsumi; Nishimura, Yuri; Matsuda, Satoru

doi: 10.1016/j.febslet.2011.05.011pmid: 21570977

RUN domain is present in several proteins related to the functions of Rap and Rab family GTPases. Accumulating evidence supports the hypothesis that RUN domain‐containing proteins act as a component of vesicle traffic and might be responsible for an interaction with a filamentous network linked to actin cytoskeleton or microtubules. That is to say, on one hand, RUN domains associate with Rab or Rap family proteins, on the other hand, they also might interact with motor proteins such as kinesin or myosin via intervention molecules. In this review, we summarize the background and current status of RUN domain research with an emphasis on the interaction between RUN domain and motor proteins with respect to the vesicle traffic on filamentous network.

Heemskerk, Johan W.M.; Harper, Matthew T.; Cosemans, Judith M.E.M.; Poole, Alastair W.

doi: 10.1016/j.febslet.2011.05.017pmid: 21596041

Platelets tightly regulate haemostasis and arterial thrombosis. Protein kinase C (PKC) is involved in most platelet responses implicated in thrombus formation. Recent pharmacological and mouse gene knockout approaches show that the conventional PKC isoforms and the novel PKC isoforms contribute in distinct ways to these platelet responses. We hypothesize that, in platelets and other cells, the characteristic functions of PKC isoforms are established through unique activation mechanisms and unique interacting protein partners, which result in isoform‐specific patterns of substrate phosphorylation. For identifying the substrate proteins in a living cell, new methodology is available and discussed.

Puthiyaveetil, Sujith

doi: 10.1016/j.febslet.2011.04.076pmid: 21557941

State transitions are acclimatory responses to changes in light quality in photosynthesis. They involve the redistribution of absorbed excitation energy between photosystems I and II. In plants and green algae, this redistribution is produced by reversible phosphorylation of the chloroplast light harvesting complex II (LHC II). The LHC II kinase is activated by reduced plastoquinone (PQ) in photosystem II‐specific low light. In high light, when PQ is also reduced, LHC II kinase becomes inactivated by thioredoxin. Based on newly identified amino acid sequence features of LHC II kinase and other considerations, a mechanism is suggested for its redox regulation.

Xhabija, Besa; Taylor, Gregory S.; Fujibayashi, Akemi; Sekiguchi, Kiyotoshi; Vacratsis, Panayiotis O.

doi: 10.1016/j.febslet.2011.04.016pmid: 21510942

RME8 and EGFR colocalize by fluorescence microscopy (View interaction)

Lowther, Jonathan; Charmier, Guillaume; Raman, Marine C.; Ikushiro, Hiroko; Hayashi, Hideyuki; Campopiano, Dominic J.

doi: 10.1016/j.febslet.2011.04.013pmid: 21514297

SPT binds to SPT by molecular sieving (View interaction)

Li, Yun; Wang, Pengcheng; Zhuang, Yuan; Lin, Huan; Li, Yehua; Liu, Ling; Meng, Qinghang; Cui, Ting; Liu, Jing; Li, Zhen

doi: 10.1016/j.febslet.2011.04.051pmid: 21536037

Adiponectin physically interacts with Adiponectin by comigration in gel electrophoresis (View Interaction 1, 2) Adiponectin physically interacts with Adiponectin by cosedimentation through density gradient (View interaction)

Takahashi, Yuga; Shimokawa, Noriaki; Esmaeili-Mahani, Saeed; Morita, Akihito; Masuda, Hiroko; Iwasaki, Toshiharu; Tamura, Jun'ichi; Haglund, Kaisa; Koibuchi, Noriyuki

doi: 10.1016/j.febslet.2011.04.056pmid: 21570973

c‐Cbl physically interacts with TrkA by anti bait coimmunoprecipitation (View interaction)

Leineweber, Sarah; Schönig, Sarah; Seeger, Karsten

doi: 10.1016/j.febslet.2011.04.071pmid: 21570975

mvWFA2 binds to mFNIII‐9 by surface plasmon resonance (View interaction)

Farkas, Daniel; Hansson, Örjan

doi: 10.1016/j.febslet.2011.04.073pmid: 21570396

Pc and PsaF bind by nuclear magnetic resonance (View interaction)