View source for 4zdv


==Crystal structure of LC3 in complex with FAM134B LIR==
<StructureSection load='4zdv' size='340' side='right'caption='[[4zdv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zdv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdv OCA], [https://pdbe.org/4zdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdv RCSB], [https://www.ebi.ac.uk/pdbsum/4zdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MLP3A_HUMAN MLP3A_HUMAN] Involved in formation of autophagosomal vacuoles (autophagosomes).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The endoplasmic reticulum (ER) is the largest intracellular endomembrane system, enabling protein and lipid synthesis, ion homeostasis, quality control of newly synthesized proteins and organelle communication. Constant ER turnover and modulation is needed to meet different cellular requirements and autophagy has an important role in this process. However, its underlying regulatory mechanisms remain unexplained. Here we show that members of the FAM134 reticulon protein family are ER-resident receptors that bind to autophagy modifiers LC3 and GABARAP, and facilitate ER degradation by autophagy ('ER-phagy'). Downregulation of FAM134B protein in human cells causes an expansion of the ER, while FAM134B overexpression results in ER fragmentation and lysosomal degradation. Mutant FAM134B proteins that cause sensory neuropathy in humans are unable to act as ER-phagy receptors. Consistently, disruption of Fam134b in mice causes expansion of the ER, inhibits ER turnover, sensitizes cells to stress-induced apoptotic cell death and leads to degeneration of sensory neurons. Therefore, selective ER-phagy via FAM134 proteins is indispensable for mammalian cell homeostasis and controls ER morphology and turnover in mice and humans.

Regulation of endoplasmic reticulum turnover by selective autophagy.,Khaminets A, Heinrich T, Mari M, Grumati P, Huebner AK, Akutsu M, Liebmann L, Stolz A, Nietzsche S, Koch N, Mauthe M, Katona I, Qualmann B, Weis J, Reggiori F, Kurth I, Hubner CA, Dikic I Nature. 2015 Jun 3. doi: 10.1038/nature14498. PMID:26040720<ref>PMID:26040720</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zdv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Akutsu M]]
[[Category: Dikic I]]
[[Category: Grumati P]]
[[Category: Khaminets A]]