Log in

Relevant bibliographies by topics / Atg1 protein kinase

Contents

Journal articles
Dissertations / Theses

Academic literature on the topic 'Atg1 protein kinase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Atg1 protein kinase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Atg1 protein kinase"

1

Sawa-Makarska, Justyna, Verena Baumann, Nicolas Coudevylle, et al. "Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds for membrane formation." Science 369, no. 6508 (2020): eaaz7714. http://dx.doi.org/10.1126/science.aaz7714.

Full text

Abstract:

Autophagosomes form de novo in a manner that is incompletely understood. Particularly enigmatic are autophagy-related protein 9 (Atg9)–containing vesicles that are required for autophagy machinery assembly but do not supply the bulk of the autophagosomal membrane. In this study, we reconstituted autophagosome nucleation using recombinant components from yeast. We found that Atg9 proteoliposomes first recruited the phosphatidylinositol 3-phosphate kinase complex, followed by Atg21, the Atg2-Atg18 lipid transfer complex, and the E3-like Atg12–Atg5-Atg16 complex, which promoted Atg8 lipidation. F

APA, Harvard, Vancouver, ISO, and other styles

2

Hegedűs, Krisztina, Péter Nagy, Zoltán Gáspári, and Gábor Juhász. "The Putative HORMA Domain Protein Atg101 Dimerizes and Is Required for Starvation-Induced and Selective Autophagy inDrosophila." BioMed Research International 2014 (2014): 1–13. http://dx.doi.org/10.1155/2014/470482.

Full text

Abstract:

The large-scale turnover of intracellular material including organelles is achieved by autophagy-mediated degradation in lysosomes. Initiation of autophagy is controlled by a protein kinase complex consisting of an Atg1-family kinase, Atg13, FIP200/Atg17, and the metazoan-specific subunit Atg101. Here we show that loss of Atg101 impairs both starvation-induced and basal autophagy inDrosophila. This leads to accumulation of protein aggregates containing the selective autophagy cargo ref(2)P/p62. Mapping experiments suggest that Atg101 binds to the N-terminal HORMA domain of Atg13 and may also i

APA, Harvard, Vancouver, ISO, and other styles

3

Chang, Yu-Yun, and Thomas P. Neufeld. "An Atg1/Atg13 Complex with Multiple Roles in TOR-mediated Autophagy Regulation." Molecular Biology of the Cell 20, no. 7 (2009): 2004–14. http://dx.doi.org/10.1091/mbc.e08-12-1250.

Full text

Abstract:

The TOR kinases are conserved negative regulators of autophagy in response to nutrient conditions, but the signaling mechanisms are poorly understood. Here we describe a complex containing the protein kinase Atg1 and the phosphoprotein Atg13 that functions as a critical component of this regulation in Drosophila. We show that knockout of Atg1 or Atg13 results in a similar, selective defect in autophagy in response to TOR inactivation. Atg1 physically interacts with TOR and Atg13 in vivo, and both Atg1 and Atg13 are phosphorylated in a nutrient-, TOR- and Atg1 kinase-dependent manner. In contra

APA, Harvard, Vancouver, ISO, and other styles

4

Cheong, Heesun, Usha Nair, Jiefei Geng, and Daniel J. Klionsky. "The Atg1 Kinase Complex Is Involved in the Regulation of Protein Recruitment to Initiate Sequestering Vesicle Formation for Nonspecific Autophagy in Saccharomyces cerevisiae." Molecular Biology of the Cell 19, no. 2 (2008): 668–81. http://dx.doi.org/10.1091/mbc.e07-08-0826.

Full text

Abstract:

Autophagy is the major degradative process for recycling cytoplasmic constituents and eliminating unnecessary organelles in eukaryotic cells. Most autophagy-related (Atg) proteins are recruited to the phagophore assembly site (PAS), a proposed site for vesicle formation during either nonspecific or specific types of autophagy. Therefore, appropriate recruitment of Atg proteins to this site is critical for their function in autophagy. Atg11 facilitates PAS recruitment for the cytoplasm-to-vacuole targeting pathway, which is a specific, autophagy-like process that occurs under vegetative conditi

APA, Harvard, Vancouver, ISO, and other styles

5

Kabeya, Yukiko, Yoshiaki Kamada, Misuzu Baba, Hirosato Takikawa, Mitsuru Sasaki, and Yoshinori Ohsumi. "Atg17 Functions in Cooperation with Atg1 and Atg13 in Yeast Autophagy." Molecular Biology of the Cell 16, no. 5 (2005): 2544–53. http://dx.doi.org/10.1091/mbc.e04-08-0669.

Full text

Abstract:

In eukaryotic cells, nutrient starvation induces the bulk degradation of cellular materials; this process is called autophagy. In the yeast Saccharomyces cerevisiae, most of the ATG (autophagy) genes are involved in not only the process of degradative autophagy, but also a biosynthetic process, the cytoplasm to vacuole (Cvt) pathway. In contrast, the ATG17 gene is required specifically in autophagy. To better understand the function of Atg17, we have performed a biochemical characterization of the Atg17 protein. We found that the atg17Δ mutant under starvation condition was largely impaired in

APA, Harvard, Vancouver, ISO, and other styles

6

Mesquita, Ana, Luis C. Tábara, Oscar Martinez-Costa, Natalia Santos-Rodrigo, Olivier Vincent, and Ricardo Escalante. "Dissecting the function of Atg1 complex in Dictyostelium autophagy reveals a connection with the pentose phosphate pathway enzyme transketolase." Open Biology 5, no. 8 (2015): 150088. http://dx.doi.org/10.1098/rsob.150088.

Full text

Abstract:

The network of protein–protein interactions of the Dictyostelium discoideum autophagy pathway was investigated by yeast two-hybrid screening of the conserved autophagic proteins Atg1 and Atg8. These analyses confirmed expected interactions described in other organisms and also identified novel interactors that highlight the complexity of autophagy regulation. The Atg1 kinase complex, an essential regulator of autophagy, was investigated in detail here. The composition of the Atg1 complex in D. discoideum is more similar to mammalian cells than to Saccharomyces cerevisiae as, besides Atg13, it

APA, Harvard, Vancouver, ISO, and other styles

7

Kamada, Yoshiaki, Ken-ichi Yoshino, Chika Kondo, et al. "Tor Directly Controls the Atg1 Kinase Complex To Regulate Autophagy." Molecular and Cellular Biology 30, no. 4 (2009): 1049–58. http://dx.doi.org/10.1128/mcb.01344-09.

Full text

Abstract:

ABSTRACT Autophagy is a bulk proteolytic process that is indispensable for cell survival during starvation. Autophagy is induced by nutrient deprivation via inactivation of the rapamycin-sensitive Tor complex1 (TORC1), a protein kinase complex regulating cell growth in response to nutrient conditions. However, the mechanism by which TORC1 controls autophagy and the direct target of TORC1 activity remain unclear. Atg13 is an essential regulatory component of autophagy upstream of the Atg1 kinase complex, and here we show that yeast TORC1 directly phosphorylates Atg13 at multiple Ser residues. A

APA, Harvard, Vancouver, ISO, and other styles

8

Chang, Yu-Yun, Gábor Juhász, Pankuri Goraksha-Hicks, et al. "Nutrient-dependent regulation of autophagy through the target of rapamycin pathway." Biochemical Society Transactions 37, no. 1 (2009): 232–36. http://dx.doi.org/10.1042/bst0370232.

Full text

Abstract:

In response to nutrient deficiency, eukaryotic cells activate macroautophagy, a degradative process in which proteins, organelles and cytoplasm are engulfed within unique vesicles called autophagosomes. Fusion of these vesicles with the endolysosomal compartment leads to breakdown of the sequestered material into amino acids and other simple molecules, which can be used as nutrient sources during periods of starvation. This process is driven by a group of autophagy-related (Atg) proteins, and is suppressed by TOR (target of rapamycin) signalling under favourable conditions. Several distinct ki

APA, Harvard, Vancouver, ISO, and other styles

9

Tekinay, Turgay, Mary Y. Wu, Grant P. Otto, O. Roger Anderson, and Richard H. Kessin. "Function of the Dictyostelium discoideum Atg1 Kinase during Autophagy and Development." Eukaryotic Cell 5, no. 10 (2006): 1797–806. http://dx.doi.org/10.1128/ec.00342-05.

Full text

Abstract:

ABSTRACT When starved, the amoebae of Dictyostelium discoideum initiate a developmental process that results in the formation of fruiting bodies in which stalks support balls of spores. The nutrients and energy necessary for development are provided by autophagy. Atg1 is a protein kinase that regulates the induction of autophagy in the budding yeast Saccharomyces cerevisiae. In addition to a conserved kinase domain, Dictyostelium Atg1 has a C-terminal region that has significant homology to the Caenorhabditis elegans and mammalian Atg1 homologues but not to the budding yeast Atg1. We investiga

APA, Harvard, Vancouver, ISO, and other styles

10

Chan, Edmond Y. W., Andrea Longatti, Nicole C. McKnight, and Sharon A. Tooze. "Kinase-Inactivated ULK Proteins Inhibit Autophagy via Their Conserved C-Terminal Domains Using an Atg13-Independent Mechanism." Molecular and Cellular Biology 29, no. 1 (2008): 157–71. http://dx.doi.org/10.1128/mcb.01082-08.

Full text

Abstract:

ABSTRACT The yeast Atg1 serine/threonine protein kinase and its mammalian homologs ULK1 and ULK2 play critical roles during the activation of autophagy. Previous studies have demonstrated that the conserved C-terminal domain (CTD) of ULK1 controls the regulatory function and localization of the protein. Here, we explored the role of kinase activity and intramolecular interactions to further understand ULK function. We demonstrate that the dominant-negative activity of kinase-dead mutants requires a 7-residue motif within the CTD. Our data lead to a model in which the functions of ULK1 and ULK2

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "Atg1 protein kinase"

1

Yeh, Yuh-Ying. "The regulation of Atg1 protein kinase activity is important to the autophagy process in Saccharomyces cerevisiae." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1290439442.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Budovskaya, Yelena V. "An Evaluationary Proteomics Approach for the Identification of Substrates of the Camp-Dependent Protein Kinase in Saccharomyces Cerevisiae." Connect to this title online, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1104152442.

Full text

Abstract:

Thesis (Ph. D.)--Ohio State University, 2005.<br>Title from first page of PDF file. Document formatted into pages; contains xiv, 128 p.; also includes graphics (some col.) Includes bibliographical references (p. 117-132).

APA, Harvard, Vancouver, ISO, and other styles

3

Crajoinas, Renato de Oliveira. "Papel da via receptor AT1/proteina Gi e da proteína motora miosina IIA no aumento da atividade do NHE3 pela angiotensina II em túbulo proximal renal." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/5/5166/tde-18122017-092553/.

Full text

Abstract:

A isoforma 3 do trocador Na+ /H+ (NHE3), presente em membrana apical, é a proteína de transporte que medeia a maior parte da reabsorção de NaCl e NaHCO3- em túbulo proximal renal. A fosforilação direta do NHE3 por PKA na serina 552 é um dos mecanismos pelos quais a sua atividade pode ser inibida. A ligação da angiotensina II (Ang II) ao receptor AT1 (AT1R) em túbulo proximal estimula a atividade do NHE3 por diferentes vias de sinalização. Entretanto, não foram ainda bem estabelecidos os efeitos da ativação da via AT1R/Gi, com consequente diminuição nos níveis de cAMP, na regulação do NHE3. A A

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!