نتایج جستجو برای: h2 eb1

تعداد نتایج: 24919  

2009
Marija Zanic Jeffrey H. Stear Anthony A. Hyman Jonathon Howard

Plus-end-tracking proteins (+TIPs) are localized at the fast-growing, or plus end, of microtubules, and link microtubule ends to cellular structures. One of the best studied +TIPs is EB1, which forms comet-like structures at the tips of growing microtubules. The molecular mechanisms by which EB1 recognizes and tracks growing microtubule ends are largely unknown. However, one clue is that EB1 ca...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2009
Ram Dixit Brian Barnett Jacob E Lazarus Mariko Tokito Yale E Goldman Erika L F Holzbaur

Microtubules are polarized polymers that exhibit dynamic instability, with alternating phases of elongation and shortening, particularly at the more dynamic plus-end. Microtubule plus-end tracking proteins (+TIPs) localize to and track with growing microtubule plus-ends in the cell. +TIPs regulate microtubule dynamics and mediate interactions with other cellular components. The molecular mechan...

2011
Benjamin Vitre Frédéric M. Coquelle Claire Heichette Cyrille Garnier Denis Chrétien Isabelle Arnal

1 EB1 promotes microtubule dynamics and regulates tubulin sheet closure in vitro. End binding 1 (EB1) is a plus-end-tracking protein (+TIP) that localizes to microtubule plus ends where it modulates their dynamics and interactions with intracellular organelles 1, 2. Although the regulating activity of EB1 on microtubule dynamics has been studied in cells 3-6 and purified systems 7-13 , the mole...

2015
Chi-Ting Chiu Chih-Kai Liao Chien-Chang Shen Tswen-Kei Tang Guey-Mei Jow Hwai-Shi Wang Jiahn-Chun Wu

HYS-32 is a novel derivative of combretastatin-A4 (CA-4) previously shown to induce microtubule coiling in rat primary astrocytes. In this study, we further investigated the signaling mechanism and EB1, a microtubule-associated end binding protein, involved in HYS-32-induced microtubule catastrophes. Confocal microscopy with double immunofluorescence staining revealed that EB1 accumulates at th...

Journal: :Current Biology 1999
Lisbeth Berrueta Jennifer S. Tirnauer Scott C. Schuyler David Pellman Barbara E. Bierer

Human EB1 is a highly conserved protein that binds to the carboxyl terminus of the human adenomatous polyposis coli (APC) tumor suppressor protein [1], a domain of APC that is commonly deleted in colorectal neoplasia [2]. EB1 belongs to a family of microtubule-associated proteins that includes Schizosaccharomyces pombe Mal3 [3] and Saccharomyces cerevisiae Bim1p [4]. Bim1p appears to regulate t...

Journal: :Journal of cell science 2007
Alistair N Hume Dmitry S Ushakov Abul K Tarafder Michael A Ferenczi Miguel C Seabra

Melanosome transport in melanocytes is a model system for the study of cytoskeletal regulation of intracellular transport. Melanophilin (Mlph) is a Rab27a- and myosin Va (MyoVa)-binding protein that regulates this process. Using yeast two-hybrid screening, we identified MT plus-end binding protein (EB1) as a melanocyte-expressed Mlph-interacting protein. To address the role of EB1 versus Rab27a...

Journal: :The Journal of Cell Biology 2002
Stephen L. Rogers Gregory C. Rogers David J. Sharp Ronald D. Vale

EB1 is an evolutionarily conserved protein that localizes to the plus ends of growing microtubules. In yeast, the EB1 homologue (BIM1) has been shown to modulate microtubule dynamics and link microtubules to the cortex, but the functions of metazoan EB1 proteins remain unknown. Using a novel preparation of the Drosophila S2 cell line that promotes cell attachment and spreading, we visualized dy...

Journal: :Journal of cell science 2011
Jacob M Schrøder Jesper Larsen Yulia Komarova Anna Akhmanova Rikke I Thorsteinsson Ilya Grigoriev Robert Manguso Søren T Christensen Stine F Pedersen Stefan Geimer Lotte B Pedersen

The microtubule (MT) plus-end-tracking protein EB1 is required for assembly of primary cilia in mouse fibroblasts, but the mechanisms involved and the roles of the related proteins EB2 and EB3 in ciliogenesis are unknown. Using protein depletion experiments and expression of dominant-negative constructs we show here that EB1 and EB3, but not EB2, are required for assembly of primary cilia in cu...

2016
Yijun Zhang Youguang Luo Rui Lyu Jie Chen Ruming Liu Dengwen Li Min Liu Jun Zhou

Cell migration, a complex process critical for tumor progression and metastasis, requires a dynamic crosstalk between microtubules (MTs) and focal adhesions (FAs). However, the molecular mechanisms underlying this event remain elusive. Herein we identify the proto-oncogenic protein Src as an important player in the regulation of the MT-FA crosstalk. Src interacts with and phosphorylates end-bin...

2014
Karolina Leśniewska Emma Warbrick Hiroyuki Ohkura

EB1 is a conserved protein that plays a central role in regulating microtubule dynamics and organization. It binds directly to microtubule plus ends and recruits other plus end-localizing proteins. Most EB1-binding proteins contain a Ser-any residue-Ile-Pro (SxIP) motif. Here we describe the isolation of peptide aptamers with optimized versions of this motif by screening for interaction with th...

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