Cargando…

GRASP65 controls the cis Golgi integrity in vivo

GRASP65 and GRASP55 are peripheral Golgi proteins localized to cis and medial/trans cisternae, respectively. They are implicated in diverse aspects of protein transport and structure related to the Golgi complex, including the stacking of the Golgi stack and/or the linking of mammalian Golgi stacks...

Descripción completa

Detalles Bibliográficos
Autores principales:	Veenendaal, Tineke, Jarvela, Tim, Grieve, Adam G., van Es, Johan H., Linstedt, Adam D., Rabouille, Catherine
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	The Company of Biologists 2014
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4058077/ https://www.ncbi.nlm.nih.gov/pubmed/24795147 http://dx.doi.org/10.1242/bio.20147757

Ejemplares similares

GRASP: A Multitasking Tether
por: Rabouille, Catherine, et al.
Publicado: (2016)

The function of GORASPs in Golgi apparatus organization in vivo
por: Grond, Rianne, et al.
Publicado: (2020)

Correction: The function of GORASPs in Golgi apparatus organization in vivo
por: Grond, Rianne, et al.
Publicado: (2020)

Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization
por: Jarvela, Timothy, et al.
Publicado: (2014)

Knockout of the Golgi stacking proteins GRASP55 and GRASP65 impairs Golgi structure and function
por: Bekier, Michael E., et al.
Publicado: (2017)

Manganese-induced Trafficking and Turnover of the cis-Golgi Glycoprotein GPP130
por: Mukhopadhyay, Somshuvra, et al.
Publicado: (2010)

DjA1 maintains Golgi integrity via interaction with GRASP65
por: Li, Jie, et al.
Publicado: (2019)

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking
por: Xiang, Yi, et al.
Publicado: (2010)

Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure
por: Zhang, Yijun, et al.
Publicado: (2020)

Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly
por: Tang, Danming, et al.
Publicado: (2012)

In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation
por: Aguilera-Gomez, Angelica, et al.
Publicado: (2016)

COPII–Golgi protein interactions regulate COPII coat assembly and Golgi size
por: Guo, Yusong, et al.
Publicado: (2006)

Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65
por: Xiang, Yi, et al.
Publicado: (2013)

Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking
por: Tang, Danming, et al.
Publicado: (2016)

ERK regulates Golgi and centrosome orientation towards the leading edge through GRASP65
por: Bisel, Blaine, et al.
Publicado: (2008)

Phosphorylation of Golgi Peripheral Membrane Protein Grasp65 Is an Integral Step in the Formation of the Human Cytomegalovirus Cytoplasmic Assembly Compartment
por: Rebmann, G. Michael, et al.
Publicado: (2016)

GRASPs in Golgi Structure and Function
por: Zhang, Xiaoyan, et al.
Publicado: (2016)

Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis
por: Lane, Jon D., et al.
Publicado: (2002)

Induced oligomerization targets Golgi proteins for degradation in lysosomes
por: Tewari, Ritika, et al.
Publicado: (2015)

Journeys through the Golgi—taking stock in a new era
por: Emr, Scott, et al.
Publicado: (2009)

Caspase cleavage of the Golgi stacking factor GRASP65 is required for Fas/CD95-mediated apoptosis
por: Cheng, J P X, et al.
Publicado: (2010)

GRASPing for consensus about the Golgi apparatus
por: Burd, Christopher G.
Publicado: (2021)

Editorial: Golgi Pathology in Neurodegenerative Diseases
por: Rabouille, Catherine, et al.
Publicado: (2016)

GRASP65 gets the chop
por: Wells, William A.
Publicado: (2002)

A stress assembly that confers cell viability by preserving ERES components during amino-acid starvation
por: Zacharogianni, Margarita, et al.
Publicado: (2014)

Manganese induces oligomerization to promote down-regulation of the intracellular trafficking receptor used by Shiga toxin
por: Tewari, Ritika, et al.
Publicado: (2014)

The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic
por: Behnia, Rudy, et al.
Publicado: (2007)

Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130
por: Puthenveedu, Manojkumar A., et al.
Publicado: (2001)

Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network
por: Sengupta, Debrup, et al.
Publicado: (2009)

Stress-induced phase separation of ERES components into Sec bodies precedes ER exit inhibition in mammalian cells
por: van Leeuwen, Wessel, et al.
Publicado: (2022)

Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles
por: Haase, Georg, et al.
Publicado: (2015)

New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution
por: Mendes, Luís F. S., et al.
Publicado: (2016)

The Golgi stacking protein GRASP55 is targeted by the natural compound prodigiosin
por: Berning, Lena, et al.
Publicado: (2023)

Recycling glycoproteins do not return to the cis-Golgi
Publicado: (1988)

GRASP55 regulates intra‐Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis
por: Pothukuchi, Prathyush, et al.
Publicado: (2021)

Loss of a Clueless-dGRASP complex results in ER stress and blocks Integrin exit from the perinuclear endoplasmic reticulum in Drosophila larval muscle
por: Wang, Zong-Heng, et al.
Publicado: (2015)

The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi
Publicado: (1991)

Antibodies to rat pancreas Golgi subfractions: identification of a 58- kD cis-Golgi protein
Publicado: (1987)

Characterization of a cis-Golgi matrix protein, GM130
Publicado: (1995)

e-GRASP: an integrated evolutionary and GRASP resource for exploring disease associations
por: Karim, Sajjad, et al.
Publicado: (2016)

Cannot write session to /tmp/vufind_sessions/sess_mtmc71cf5dp3aoad9ernqs9jak