Results 51 to 60 of about 9,354,840 (235)

Structural determinants of Rab11 activation by the guanine nucleotide exchange factor SH3BP5

Nature Communications, 2018
Rab11 GTPases are involved in various cellular processes but their activation by guanine nucleotide exchange factors (GEFs) is not fully understood.
Meredith L. Jenkins, Jean Piero Margaria, Jordan T. B. Stariha, Reece M. Hoffmann, Jacob A. McPhail, David J. Hamelin, Martin J. Boulanger, Emilio Hirsch, John E. Burke   +8 more
doaj   +1 more source

This Is the End: Regulation of Rab7 Nucleotide Binding in Endolysosomal Trafficking and Autophagy

Frontiers in Cell and Developmental Biology, 2018
Rab7 – or in yeast, Ypt7p – governs membrane trafficking in the late endocytic and autophagic pathways. Rab7 also regulates mitochondrion-lysosome contacts, the sites of mitochondrial fission.
Christopher Stroupe
doaj   +1 more source

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

FEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes, Jan Brysch, Carmen Gelze, Lilli Meier, Daniel Kümmel   +4 more
wiley   +1 more source

Activation of an Estrogen/ Estrogen Receptor Signaling by BIG3 Through Its Inhibitory Effect on Nuclear Transport of PHB2/REA in Breast Cancer [PDF]

, 2009
Breast cancer is known to be a hormone-dependent disease, and estrogens through an interaction with estrogen receptor (ER) enhance the proliferative and metastatic activity of breast tumor cells.
Yusuke Nakamura, Tomomi Ueki, Miki Akiyama, Meng-Lay Lin, Arata Shimo, Jae-Hyun Park, Yataro Daigo, Toyomasa Katagiri, Tatsuhiko Tsunoda, Jung-Won Kim, Toshihiko Nishidate   +10 more
core  

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

Exploring the correlation between the sequence composition of the nucleotide binding G5 loop of the FeoB GTPase domain (NFeoB) and intrinsic rate of GDP release

Bioscience Reports, 2014
GDP release from GTPases is usually extremely slow and is in general assisted by external factors, such as association with guanine exchange factors or membrane-embedded GPCRs (G protein-coupled receptors), which accelerate the release of GDP by several ...
Amy P. Guilfoyle, Chandrika N. Deshpande, Gerhard Schenk, Megan J. Maher, Mika Jormakka   +4 more
doaj   +1 more source

Mechanism of the exchange reaction in HRAS from multiscale modeling. [PDF]

PLoS ONE, 2014
HRAS regulates cell growth promoting signaling processes by cycling between active (GTP-bound) and inactive (GDP-bound) states. Understanding the transition mechanism is central for the design of small molecules to inhibit the formation of RAS-driven ...
Abhijeet Kapoor, Alex Travesset
doaj   +1 more source

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

FEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source

The domain architecture of large guanine nucleotide exchange factors for the small GTP-binding protein Arf

BMC Genomics, 2005
Background Small G proteins, which are essential regulators of multiple cellular functions, are activated by guanine nucleotide exchange factors (GEFs) that stimulate the exchange of the tightly bound GDP nucleotide by GTP.
Geldner Niko, Shields David J, Cohen Jean, Joubert Alexandra, Biou Valerie, Mouratou Barbara, Jürgens Gerd, Melançon Paul, Cherfils Jacqueline   +8 more
doaj   +1 more source

Covalent Inhibitors Allosterically Block the Activation of Rho Family Proteins and Suppress Cancer Cell Invasion

Advanced Science, 2020
The Rho family GTPases are crucial drivers of tumor growth and metastasis. However, it is difficult to develop GTPases inhibitors due to a lack of well‐characterized binding pockets for compounds.
Zhongya Sun, Hao Zhang, Yuanyuan Zhang, Liping Liao, Wen Zhou, Fengcai Zhang, Fulin Lian, Jing Huang, Pan Xu, Rukang Zhang, Wenchao Lu, Mingrui Zhu, Hongru Tao, Feng Yang, Hong Ding, Shijie Chen, Liyan Yue, Bing Zhou, Naixia Zhang, Minjia Tan, Hualiang Jiang, Kaixian Chen, Bo Liu, Chuanpeng Liu, Yongjun Dang, Cheng Luo   +25 more
doaj   +1 more source