SEC22A

Last update 08 May 2025

Basic Info

Synonyms

SEC22 homolog A, vesicle trafficking protein, SEC22 vesicle-trafficking protein homolog A, SEC22 vesicle-trafficking protein-like 2

+ [3]

Introduction

May be involved in vesicle transport between the ER and the Golgi complex.

100 Clinical Results associated with SEC22A

100 Translational Medicine associated with SEC22A

0 Patents (Medical) associated with SEC22A

Literatures (Medical) associated with SEC22A

15 Dec 2023·Development

ARRDC5 deficiency impairs spermatogenesis by affecting SUN5 and NDC1

Article

Author: Chen, Biaobang ; Luo, Yuxi ; Liu, Ruyi ; Wang, Lei ; Zeng, Yang ; Qu, Ronggui ; Xu, Fangzhou ; Li, Qun ; Sang, Qing ; Zhang, Zhihua ; Mu, Jian

ABSTRACTSperm with normal morphology and motility are essential for successful fertilization, and the strong attachment of the sperm head-tail coupling apparatus to the nuclear envelope during spermatogenesis is required to ensure the integrity of sperm for capacitation and fertilization. Here, we report that Arrdc5 is associated with spermatogenesis. The Arrdc5 knockout mouse model showed male infertility characterized by a high bent-head rate and reduced motility in sperm, which led to capacitation defects and subsequent fertilization failure. Through mass spectrometry, we found that ARRDC5 affects spermatogenesis by affecting NDC1 and SUN5. We further found that ARRDC5 might affect the vesicle-trafficking protein SEC22A-mediated transport and localization of NDC1, SUN5 and other head-tail coupling apparatus-related proteins that are responsible for initiating the attachment of the sperm head and tail. We finally performed intracytoplasmic sperm injection as a way to explore therapeutic strategies. Our findings demonstrate the essential role and the underlying molecular mechanism of ARRDC5 in anchoring the sperm head to the tail during spermatogenesis.

01 Nov 2023·Journal of Biological Chemistry

Comparative proximity biotinylation implicates the small GTPase RAB18 in sterol mobilization and biosynthesis

Article

Author: Hafiane, Anouar ; Alecki, Célia ; Handley, Mark T ; Sladek, Robert ; Kerksiek, Anja ; Chen, He ; Nilsson, Tommy ; Lebrun, Jean-Jacques ; Chicoine, Jarred ; Kyei-Boahen, Jeffrey ; von Kriegsheim, Alex ; Dale, Jessica D ; Wills, Jimi C ; Kamath, Archith ; Daliah, Girija ; Kiss, Robert S ; Heier, Martin ; Khalil, Youssef ; Clayton, Peter ; Brudenell, Tegan A ; Paci, Emanuele ; Hopes, Tayah S ; Lütjohann, Dieter ; Sheridan, Eamonn ; Aspden, Julie ; Pisaturo, Alessandro ; Martin, Cyril ; Aligianis, Irene A

Loss of functional RAB18 causes the autosomal recessive condition Warburg Micro syndrome. To better understand this disease, we used proximity biotinylation to generate an inventory of potential RAB18 effectors. A restricted set of 28 RAB18 interactions were dependent on the binary RAB3GAP1-RAB3GAP2 RAB18-guanine nucleotide exchange factor complex. Twelve of these 28 interactions are supported by prior reports, and we have directly validated novel interactions with SEC22A, TMCO4, and INPP5B. Consistent with a role for RAB18 in regulating membrane contact sites, interactors included groups of microtubule/membrane-remodeling proteins, membrane-tethering and docking proteins, and lipid-modifying/transporting proteins. Two of the putative interactors, EBP and OSBPL2/ORP2, have sterol substrates. EBP is a Δ8-Δ7 sterol isomerase, and ORP2 is a lipid transport protein. This prompted us to investigate a role for RAB18 in cholesterol biosynthesis. We found that the cholesterol precursor and EBP-product lathosterol accumulates in both RAB18-null HeLa cells and RAB3GAP1-null fibroblasts derived from an affected individual. Furthermore, de novo cholesterol biosynthesis is impaired in cells in which RAB18 is absent or dysregulated or in which ORP2 expression is disrupted. Our data demonstrate that guanine nucleotide exchange factor-dependent Rab interactions are highly amenable to interrogation by proximity biotinylation and may suggest that Micro syndrome is a cholesterol biosynthesis disorder.

01 Feb 2022·AutophagyQ1 · BIOLOGY

BECN2 (beclin 2) Negatively Regulates Inflammasome Sensors Through ATG9A-Dependent but ATG16L1- and LC3-Independent Non-Canonical Autophagy

Q1 · BIOLOGY

Article

Author: Deng, Guangtong ; Zhu, Motao ; Qian, Chen ; Liu, Xin ; Xing, Changsheng ; Wang, Helen Y. ; Fu, Chuntang ; Li, Chaoran ; Wang, Rong-Fu ; Chen, Lang

Macroautophagy/autophagy-related proteins regulate infectious and inflammatory diseases in autophagy-dependent or -independent manner. However, the role of a newly identified mammalian-specific autophagy protein-BECN2 (beclin 2) in innate immune regulation is largely unknown. Here we showed that loss of BECN2 enhanced the activities of NLRP3, AIM2, NLRP1, and NLRC4 inflammasomes upon ligand stimulations. Mechanistically, BECN2 interacted with inflammasome sensors and mediated their degradation through a ULK1- and ATG9A-dependent, but BECN1-WIPI2-ATG16L1-LC3-independent, non-canonical autophagic pathway. BECN2 recruited inflammasome sensors on ATG9A⁺ vesicles to form a complex (BECN2-ATG9A-sensors) upon ULK1 activation. Three soluble NSF attachment protein receptor (SNARE) proteins (SEC22A, STX5, and STX6) were further shown to mediate the BECN2-ATG9A-dependent inflammasome sensor degradation. Loss of BECN2 promoted alum-induced peritonitis, which could be rescued by the ablation of CASP1 in Becn2-deficient mice. Hence, BECN2 negatively regulated inflammasome activation to control inflammation, serving as a potential therapeutic target for the treatment of infectious and inflammatory diseases.Abbreviations: AIM2: absent in melanoma 2; ATG: autophagy related; BECN1: beclin 1; BMDC: bone marrow-derived dendritic cells; BMDM: bone marrow-derived macrophages; CASP1: caspase 1; CQ: chloroquine; gMDSC: granulocytic myeloid-derived suppressor cells; IL: interleukin; LPS: lipopolysaccharide; MAP1LC3B: microtubule associated protein 1 light chain 3 beta; mMDSC: monocytic myeloid-derived suppressor cells; NLRC4: NLR family CARD domain containing 4; NLRP1: NLR family pyrin domain containing 1; NLRP3: NLR family pyrin domain containing 3; PECs: peritoneal exudate cells; PYCARD/ASC: apoptosis-associated speck-like protein containing a caspase activation and recruitment domain; SNAREs: soluble NSF attachment protein receptors; STX5: syntaxin 5; STX6: syntaxin 6; ULK1: unc-51 like autophagy activating kinase 1; WIPI: WD repeat domain, phosphoinositide interacting.

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SEC22A

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