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Search results 101 to 119 out of 119 for Plekhm1

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Type Details Score
Publication
First Author: Nah J
Year: 2021
Journal: Exp Mol Med
Title: The roles of the inhibitory autophagy regulator Rubicon in the heart: A new therapeutic target to prevent cardiac cell death.
Volume: 53
Issue: 4
Pages: 528-536
Publication
First Author: Chang C
Year: 2019
Journal: Mol Cell
Title: Bidirectional Control of Autophagy by BECN1 BARA Domain Dynamics.
Volume: 73
Issue: 2
Pages: 339-353.e6
Publication
First Author: Cheng X
Year: 2017
Journal: Mol Cell
Title: Pacer Mediates the Function of Class III PI3K and HOPS Complexes in Autophagosome Maturation by Engaging Stx17.
Volume: 65
Issue: 6
Pages: 1029-1043.e5
Publication
First Author: Beltran S
Year: 2019
Journal: Mol Neurodegener
Title: Network approach identifies Pacer as an autophagy protein involved in ALS pathogenesis.
Volume: 14
Issue: 1
Pages: 14
Protein Domain
Type: Family
Description: FAM98A, B and C are glycine-rich proteins found from worms to humans. FAM98A contains a tubulin-binding calponin homology domain. It interacts with PLEKHM1 and functions in lysosome positioning in osteoclasts []. FAM98A and FAM98B are included in a novel complex with DDX1 and C14orf166 and are involved in colorectal cancer progression [].
Protein Domain
Type: Domain
Description: This is the Rubicon homology domain (RH) characterised at the C-terminal of Rubicon, PLEKHM1 and Pacer, proteins that modulate late steps in autophagy [, ]. Rubicon (RUBCN) negatively regulates autophagy and endolysosomal trafficking by inhibiting PI3K complex II (PI3KC3-C2), which impairs autophagosome maturation process. Decrease in autophagy is associated to aging, then suppression of this process by Rubicon has been linked to decreased clearance of alpha-synuclein aggregates in neural tissues, impairment of liver cell homeostasis, and interstitial fibrosis in the kidney. PLEKHM1 is an adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways [, ], being involved in the suppression of endocytic transport rather than autophagosome maturation. Mutations in PLEKHM1 causes osteopetrosis []. On the other hand, Pacer (Protein associated with UVRAG as autophagy enhancer or Rubicon-like) positively regulates autophagy, promoting autophagosome maturation by facilitating the biogenesis of phosphatidylinositol 3-phosphate (PtdIns3P) in late steps of autophagy [, ]. It antagonizes RUBCN, thereby stimulating phosphatidylinositol 3-kinase activity of the PI3K/PI3KC3 complex []. Pacer is involved in neuronal autophagy, whose deficiency leads to impaired autophagy and accumulation of protein aggregates in ALS which correlates with cell death and vulnerability of motoneurons during ALS pathogenesis [].This domain contains nine conserved cysteines and one conserved histidine, which have been predicted to bind divalent zinc cations, being required for Rubicon and PLEKHM1 to interact with Rab7 [, ].
Protein
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 956  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 460  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 880  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 472  
Fragment?: false
Publication
First Author: McEwan DG
Year: 2015
Journal: Autophagy
Title: PLEKHM1: Adapting to life at the lysosome.
Volume: 11
Issue: 4
Pages: 720-2
Publication
First Author: van Wesenbeeck L
Year: 2004
Journal: J Bone Miner Res
Title: Localization of the gene causing the osteopetrotic phenotype in the incisors absent (ia) rat on chromosome 10q32.1.
Volume: 19
Issue: 2
Pages: 183-9
Protein Domain
Type: Domain
Description: PLEKHM1 is a ubiquitously expressed protein involved in the regulation of osteoclast function and bone resorption []. It may function as an adaptor protein that acts as a central hub to integrate endocytic and autophagic pathways at the lysosome []. PLEKHM1 contains an N-terminal RUN domain (RPIP8/RaP2 interacting protein 8, UNC-14 and NESCA/new molecule containing SH3 at the carboxyl-terminus), followed by a PH domain, and either a C1 domain or a DUF4206 domain at its C terminus. The RUN domain is thought to be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].
Protein
Organism: Mus musculus/domesticus
Length: 761  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1074  
Fragment?: false
Publication
First Author: Lemmon MA
Year: 2004
Journal: Biochem Soc Trans
Title: Pleckstrin homology domains: not just for phosphoinositides.
Volume: 32
Issue: Pt 5
Pages: 707-11
Publication  
First Author: Cozier GE
Year: 2004
Journal: Curr Top Microbiol Immunol
Title: Membrane targeting by pleckstrin homology domains.
Volume: 282
Pages: 49-88
Publication
First Author: Scheffzek K
Year: 2012
Journal: FEBS Lett
Title: Pleckstrin homology (PH) like domains - versatile modules in protein-protein interaction platforms.
Volume: 586
Issue: 17
Pages: 2662-73