Dataset Information

Identification of ASB1 interacting proteins by LC-MS/MS

ABSTRACT: To identify proteins that interact with ankyrin repeat and SOCS box-containing 1 (ASB1) in mouse testes, immunocoprecipitation (IP) experiments were performed and subjected to two independently LC-MS/MS analysis and Label-free quantification.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Testis

SUBMITTER: Yueshuai Guo

LAB HEAD: Bo Zheng

PROVIDER: PXD051446 | Pride | 2025-05-06

REPOSITORIES: Pride

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Publications

ASB1 engages with ELOB to facilitate SQOR ubiquitination and H<sub>2</sub>S homeostasis during spermiogenesis.

Lv Jinxing J Wu Tiantian T Xue Jiajia J Shen Cong C Gao Wenxin W Chen Xia X Guo Yueshuai Y Liu Mingxi M Yu Jun J Huang Xiaoyan X Zheng Bo B

Redox biology 20241227

Male infertility, frequently driven by oxidative stress, impacts half of infertile couples globally. Despite its significance, the precise mechanisms governing this process remain elusive. In this study, we demonstrate that ASB1, the substrate recognition subunit of a ubiquitin ligase, is highly expressed in the mouse testis. Mice lacking the Asb1 gene exhibit severe fertility impairment, characterized by oligoasthenoteratozoospermia. Subsequent investigations unveiled that Asb1 knockout (Asb1-K ...[more]

PMID: 39733518

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Project description:N-degron pathway plays an important role in the protein quality control and maintenance of cellular protein homeostasis. ZER1 and ZYG11B, the substrate receptors of the Cullin 2-RING E3 ubiquitin ligase (CRL2), recognize N-terminal (Nt) glycine degrons and participate in the Nt-myristoylation quality control through the Gly/N-degron pathway. Here we show that ZER1 and ZYG11B can also recognize small Nt-residues other than glycine. Specifically, ZER1 preferentially binds to Nt-serine, -alanine, -threonine and -cysteine over -glycine, while ZYG11B prefers Nt-glycine but also has the capacity to recognize Nt-serine, -alanine and -cysteine in vitro. Nt-serine, -alanine and -cysteine undergo Nt-acetylation by NatA, thereby shielding them from recognition by ZER1/ZYG11B in cells. We found that ZER1/ZYG11B is able to target the non-acetylation of small Nt-residue degrons for degradation in NatA-deficient cells, implicating its role in the Nt-acetylation quality control. Furthermore, we present the crystal structures of ZER1 and ZYG11B bound to various small Nt-residues and uncover the molecular mechanism of non-acetylated substrate recognition by ZER1 and ZYG11B.N-degron pathway plays an important role in the protein quality control and maintenance of cellular protein homeostasis. ZER1 and ZYG11B, the substrate receptors of the Cullin 2-RING E3 ubiquitin ligase (CRL2), recognize N-terminal (Nt) glycine degrons and participate in the Nt-myristoylation quality control through the Gly/N-degron pathway. Here we show that ZER1 and ZYG11B can also recognize small Nt-residues other than glycine. Specifically, ZER1 preferentially binds to Nt-serine, -alanine, -threonine and -cysteine over -glycine, while ZYG11B prefers Nt-glycine but also has the capacity to recognize Nt-serine, -alanine and -cysteine in vitro. Nt-serine, -alanine and -cysteine undergo Nt-acetylation by NatA, thereby shielding them from recognition by ZER1/ZYG11B in cells. We found that ZER1/ZYG11B is able to target the non-acetylation of small Nt-residue degrons for degradation in NatA-deficient cells, implicating its role in the Nt-acetylation quality control. Furthermore, we present the crystal structures of ZER1 and ZYG11B bound to various small Nt-residues and uncover the molecular mechanism of non-acetylated substrate recognition by ZER1 and ZYG11B.

Project description:Objective: Monocytes are crucially involved in inflammatory processes. In mice, different subsets of monocytes can be distinguished by the expression of Ly6C, a surface marker that is highly expressed on inflammatory monocytes (Ly6C high) and to a lesser extent on patrolling monocytes (Ly6C low). Our previous study revealed an aggravated accumulation of inflammatory Ly6C high monocytes in atherosclerotic-prone mice bearing a deficiency in suppressor of cytokine signaling (Socs)-1. In the present study, we performed a genome-wide analysis of Socs-1-dependent gene regulation in Ly6C high and Ly6C low monocytes. Methods and Results: Monocyte subsets were isolated from socs-1+/+ rag2‒/‒ ldlr–/‒ and socs-1‒/‒ rag2‒/‒ ldlr-‒/‒ mice with subsequent identification of differential regulated genes using illumina MouseWG-6 v2.0 Expression BeadChip microarrays (45,200 transcripts). Principal component analysis illustrates a distinct separation of gene expression profiles in Ly6C high and especially Ly6C low monocytes from Socs-1 deficient mice. Additionally, microarray data revealed 46 genes to be differentially regulated in a Socs-1 dependent manner in both monocytic subsets by 2-fold or more, some of which were validated by qPCR (p<0.05, n=4-6). Among them, two principal regulators of monocyte differentiation, C-X3-C chemokine receptor 1 (Cx3cr1) and colony stimulating factor 1 receptor (Csf1r), were identified to be Socs-1 dependently regulated. Especially for Csf1r a co-expression network for correlating Socs-1 dependent gene expression and protein interaction could be compiled. Furthermore, in silico analysis of a transcription factor (TF) network correlating with Socs-1 dependent mRNA expression data revealed a cluster of TF that includes Nr4a1 as well as several ets-domain proteins that may interact and thus regulate gene expression, inter alia regression of Csf1r. Conclusion: By genome-wide analysis, we could identify Cx3cr1 and Csf1r as two essential receptors mediating monocyte differentiation that are subjected to Socs-1 dependent transcription factor regulation.

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Dataset Information

Identification of ASB1 interacting proteins by LC-MS/MS

Dataset's files

Publications

ASB1 engages with ELOB to facilitate SQOR ubiquitination and H<sub>2</sub>S homeostasis during spermiogenesis.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Identification of ASB1 interacting proteins by LC-MS/MS

Dataset's files

Publications

ASB1 engages with ELOB to facilitate SQOR ubiquitination and H&lt;sub&gt;2&lt;/sub&gt;S homeostasis during spermiogenesis.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

ASB1 engages with ELOB to facilitate SQOR ubiquitination and H<sub>2</sub>S homeostasis during spermiogenesis.