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After 24 h, cells were lysed in lysis buffer(50 mM Tris-Cl pH 7.4, 150 mM NaCl, 1% NP-40, 0.5% DOC and 2 µM ATP) containing protease inhibitors (0.5 mM PMSF, 0.25 mM Pefabloc, 0.1 mM Aprotinin, 3 μM E-64 and 0.1 mM Leupeptin) and phosphatase inhibitors (1 mM Na3VO4 and 20 mM NaF). The lysates were precleared at 16,000 × g for 15 min, and 10% of the supernatant was mixed with 5x Laemmli sample buffer for input controls. The remaining lysate was incubated with a 50% slurry of anti-FLAG M2 affinity beads at 4°C for 2 h. The beads were washed three times in the same buffer used for lysis, and the captured proteins were eluted in 2x Laemmli sample buffer at 95°C for 5 min. The gels were fixed and stained with a Pierce Silver Stain for Mass Spectrometry. Proteins within the regions of interest on the gels were excised, reduced with dithiothreitol (DTT), alkylated with iodoacetamide, digested with trypsin, and dried using a SpeedVac concentrator. The dried samples were reconstituted in 0.1% formic acid and applied to an Eksigent nanoflow LC system interfaced with a Sciex 5600+ TripleTOF mass spectrometer, except that a gradient from 5% to 40% acetonitrile was used over 30 min."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Protein identification was achieved by analyzing each gel section’s tandem mass spectrometry data using Sciex ProteinPilot software (version 4.5, revision 1656). This software employs the Paragon algorithm (version 4.5.0.0, revision 1654), which searches against a Human UniProt Fasta database (captured on March 15, 2019), supplemented with common contaminating proteins (e.g., human keratins, porcine trypsin, and bovine albumin). The ProteinPilot search parameters included typical biological modifications (e.g., Met oxidation, N-terminal Gln conversion to pyroGlu, and acetylation) as variable modifications, with carboxyamidomethylation of cysteine as a fixed modification to account for the reduction and alkylation steps prior to trypsin digestion. Protein identifications are reported for proteins that matched at least two peptides at >99% confidence (<1% FDR) compared to an inverse decoy database."],"omics_type":["Proteomics"],"labhead":["Gary Thomas"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University of Pittsburgh"],"species":["Homo Sapiens (human)"],"publication":["41888583 Yang Y, Thomas L, Chen K, Villar-Pazos S, Haffey WD, D'Agostino A, Fanelli K, Choi YJ, Rathi V, Matlapudi MS, Greis KD, Thomas G. PACS1 syndrome mutation disrupts dynein-mediated cargo transport via HDAC6 and BICD2. Commun Biol. 2026 9(1):450 10.1038/s42003-026-09924-0"],"submitter_mail":["thomasg@pitt.edu"],"submitter_affiliation":["University of Pittsburgh"],"submitter_country":["United States"],"pubmed_abstract":["PACS1 syndrome is a neurodevelopmental disorder caused by a recurrent heterozygous missense mutation in PACS1 (p.R203W). We previously showed that PACS1<sup>R203W</sup> aberrantly potentiates HDAC6 activity, leading to Golgi fragmentation and neuronal deficits through an unresolved mechanism (Villar-Pazos and Thomas et al., Nature Commun. 14:6547-6564 (2023)). Here, we identify cytoplasmic dynein-1 heavy chain (DHC1) as a PACS1 interactor essential for maintaining furin localization at the trans-Golgi network. PACS1<sup>R203W</sup> induces a dynein loss-of-function phenotype that disrupts furin trafficking and Golgi organization. We demonstrate that PACS1<sup>R203W</sup>-HDAC6 recruits the adaptor BICD2, forming a complex that disperses the Golgi and impairs dynein function. Cargo motility assays revealed that PACS1<sup>R203W</sup> reduces dynein initiation frequency and velocity, defects rescued by HDAC6 inhibition or by expressing the dynein regulator Lis1. These findings uncover a pathogenic mechanism in which PACS1<sup>R203W</sup>-HDAC6-BICD2 disrupts dynein-driven transport, placing PACS1 syndrome within the broad spectrum of microtubule trafficking disorders."],"pubmed_title":["PACS1 syndrome mutation disrupts dynein-mediated cargo transport via HDAC6 and BICD2."],"pubmed_authors":["Yang Yunhan Y, Thomas Laurel L, Chen Kun K, Villar-Pazos Sabrina S, Haffey Wendy D WD, D'Agostino Andrew A, Fanelli Kayleigh K, Choi You-Jin YJ, Rathi Vihaan V, Matlapudi Maanas S MS, Greis Kenneth D KD, Thomas Gary G"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic screen of PACS1 interactors in HCT116 cells","description":"PACS1 syndrome is a neurodevelopmental disorder caused by a recurrent heterozygous missense mutation in PACS1 (p.R203W). We previously showed that PACS1R203W aberrantly potentiates HDAC6 activity, leading to Golgi fragmentation and neuronal deficits through an unresolved mechanism. To elucidate how PACS1R203W and HDAC6 disrupt Golgi positioning, we performed a proteomic screen to identify additional PACS1R203W partners involved in microtubule-based trafficking. HCT116 cells expressing FLAG-tagged PACS1R203W or PACS1 (control) underwent anti-FLAG immunoprecipitation (IP), and the co-purified proteins were analyzed by tandem mass spectrometry 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