Proteomics

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Retromer-Driven Membrane Trafficking of MOSPD2 Enables LEAP2-Induced Chemotaxis via VPS35 Interaction in Boleophthalmus pectinirostris

ABSTRACT: Our previous study demonstrated that Boleophthalmus pectinirostris MOSPD2 (BpMOSPD2) is the receptor of BpLEAP2. In subsequent experiments, we observed that BpMOSPD2 undergoes membrane translocation in the presence of BpLEAP2. However, BpMOSPD2 contains only five amino acids in its intracellular region, which greatly limits its intracellular activity. Therefore, we employed a combined immunoprecipitation–mass spectrometry (IP-MS) approach to identify potential intracellular proteins associated with BpMOSPD2, aiming to better explain the membrane translocation process of BpMOSPD2 in the presence of BpLEAP2.

INSTRUMENT(S):

ORGANISM(S): Boleophthalmus Pectinirostris

TISSUE(S): Cell Culture

SUBMITTER: tingfang Zhu  

LAB HEAD: Tingfang zhu

PROVIDER: PXD064369 | Pride | 2026-01-12

REPOSITORIES: Pride

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Publications

LEAP2 triggers retromer-mediated membrane trafficking of MOSPD2 to promote chemotaxis in teleost monocytes/macrophages.

Zhu Ting-Fang TF   Zhao Zi-Yue ZY   Fei Chen-Jie CJ   Shen Shi-Chang SC   Shao Jian-Zhong JZ   Nie Li L   Chen Jiong J  

Zoological research 20250901 5

Liver-expressed antimicrobial peptide 2 (LEAP2) is a key regulator of innate immune defense in teleosts, yet the molecular basis of its chemotactic function remains largely unidentified. <i>Boleophthalmus pectinirostris</i> MOSPD2 ( <i>Bp</i>MOSPD2) was previously identified as a candidate receptor for <i>Bp</i>LEAP2 in monocytes/macrophages (MO/MΦ). In the present study, <i>Bp</i>LEAP2 stimulation was found to trigger a retromer-dependent intracellular trafficking program essential for <i>Bp</i  ...[more]

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