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TRAPPC13 (also known as C5orf44) encodes trafficking protein particle complex subunit 13 in humans, a component of the TRAPPIII complex involved in membrane trafficking and autophagy (hall2024trappopathiesseveremultisystem pages 1-2, galindo2021cryo‐emstructureof pages 1-2). This gene identity is consistent across recent scientific literature, confirming that the protein described in UniProt as belonging to the TRAPPC13 family is indeed the metazoan-specific TRAPPIII subunit characterized in structural and functional studies (galindo2023thetrappcomplexes pages 2-3, hall2024trappopathiesseveremultisystem pages 4-5).
TRAPPC13 functions as a structural component of the TRAPPIII complex, one of two major TRAPP (Transport Protein Particle) complexes in metazoans (galindo2023thetrappcomplexes pages 1-2, galindo2023thetrappcomplexes pages 2-3). The TRAPPIII complex comprises a shared TRAPP core (TRAPPC1-7 subunits, with TRAPPC3 present twice) plus four metazoan-specific subunits: TRAPPC8, TRAPPC11, TRAPPC12, and TRAPPC13 (hall2024trappopathiesseveremultisystem pages 4-5, galindo2021cryo‐emstructureof pages 1-2). Recent cryo-electron microscopy structures at ~4-6 Å resolution have revealed that TRAPPIII adopts a distinctive triangular architecture with an elongated central core flanked by two large arms (galindo2021cryo‐emstructureof pages 1-2, galindo2021cryo‐emstructureof pages 3-4).
High-resolution cryo-EM analysis from Galindo et al. (2021) definitively positioned TRAPPC13, together with TRAPPC12, at the vertex where the TRAPPC8 and TRAPPC11 arms meet (galindo2021cryo‐emstructureof pages 1-2, galindo2021cryo‐emstructureof pages 3-4, galindo2021cryo‐emstructureof pages 7-9). This vertex represents the joint between the two large arms that extend from opposite ends of the core complex. TRAPPC8 and TRAPPC11 bind to the core through TRAPPC2 and TRAPPC2L, respectively, and their C-terminal regions extend to form the vertex where TRAPPC12 and TRAPPC13 are positioned (galindo2023thetrappcomplexes pages 5-7, galindo2021cryo‐emstructureof pages 5-7). This strategic location suggests TRAPPC13 contributes to the overall stability and organization of the triangular TRAPPIII architecture rather than directly participating in catalysis.
TRAPPC13 does not itself catalyze nucleotide exchange but rather supports the guanine nucleotide exchange factor (GEF) activity of the TRAPPIII complex toward Rab1 GTPase (galindo2023thetrappcomplexes pages 1-2, galindo2021cryo‐emstructureof pages 1-2). The catalytic site for Rab1 activation resides in the TRAPP core, specifically in TRAPPC1 and TRAPPC4, which form the active site for GDP-to-GTP exchange (galindo2023thetrappcomplexes pages 2-3, bagde2023thetrappcomplexes pages 1-3). Biochemical studies demonstrate that a "miniTRAPPIII" complex lacking TRAPPC12 and TRAPPC13 retains Rab1 GEF activity in vitro, indicating these subunits are dispensable for basal catalytic function (galindo2021cryo‐emstructureof pages 1-2, galindo2021cryo‐emstructureof pages 3-4). However, the larger TRAPPC8 and TRAPPC11 arms are essential for proper Rab1 activation in vivo, with TRAPPC8 positioned such that it contacts Rab1 bound to the core, thereby enhancing specificity and activity (galindo2021cryo‐emstructureof pages 1-2, galindo2021cryo‐emstructureof pages 7-9, galindo2021cryo‐emstructureof pages 9-10).
TRAPPC13, as an integral component of TRAPPIII, localizes to multiple compartments within the early secretory pathway (galindo2023thetrappcomplexes pages 1-2, maeda2025disease‐associatedfactorsat pages 8-9). The TRAPPIII complex functions at the endoplasmic reticulum (ER)-Golgi interface and the ER-Golgi intermediate compartment (ERGIC), where it regulates anterograde transport of cargo from the ER to the Golgi apparatus (maeda2025disease‐associatedfactorsat pages 1-2, hall2024trappopathiesseveremultisystem pages 4-5). Additionally, TRAPPIII localizes to the Golgi apparatus itself, where Rab1 activation is critical for maintaining Golgi structure and function (papaioannou2023biochemicalstructureand pages 1-2, maeda2025disease‐associatedfactorsat pages 8-9). Beyond the classical secretory pathway, TRAPPIII also functions at autophagosome formation sites, where it activates Rab1 during the initiation of macroautophagy (hall2024trappopathiesseveremultisystem pages 1-2, galindo2023thetrappcomplexes pages 1-2, galindo2021cryo‐emstructureof pages 9-10).
The TRAPPIII complex acts on membrane surfaces rather than in the cytosol, consistent with its role in activating prenylated Rab GTPases that are anchored to lipid bilayers (galindo2021cryo‐emstructureof pages 10-12, galindo2021cryo‐emstructureof pages 9-10). Biochemical reconstitution experiments demonstrate that TRAPPIII exhibits enhanced GEF activity toward membrane-bound Rab1 compared to soluble Rab1, emphasizing the importance of membrane association for physiological function (galindo2021cryo‐emstructureof pages 10-12, galindo2021cryo‐emstructureof pages 9-10).
TRAPPC13, through its role in TRAPPIII, is essential for ER-to-Golgi vesicular transport (hall2024trappopathiesseveremultisystem pages 1-2, galindo2023thetrappcomplexes pages 1-2). TRAPPIII activates Rab1, which serves as a master regulator of the early secretory pathway (galindo2023thetrappcomplexes pages 1-2, galindo2021cryo‐emstructureof pages 1-2). Once activated (GTP-bound), Rab1 recruits multiple effector proteins including tethering factors such as p115, GM130, and Golgin-84, which facilitate the tethering and fusion of COPII-coated vesicles with Golgi membranes (galindo2023thetrappcomplexes pages 2-3, bagde2023thetrappcomplexes pages 1-3). This Rab1-mediated tethering is crucial for the directional flow of newly synthesized proteins through the secretory pathway.
TRAPPIII plays a critical role in autophagosome formation, with TRAPPC13 contributing as a structural component of this function (hall2024trappopathiesseveremultisystem pages 1-2, galindo2023thetrappcomplexes pages 1-2, bagde2023thetrappcomplexes pages 1-3). During autophagy initiation, TRAPPIII activates Rab1 at pre-autophagosomal structures, which is essential for the recruitment of Atg1 kinase and the Atg11 tethering factor (galindo2023thetrappcomplexes pages 2-3, maeda2025disease‐associatedfactorsat pages 8-9). This Rab1 activation step is required for the first stage of macroautophagy—the formation of the isolation membrane that eventually forms the double-membrane autophagosome (galindo2023thetrappcomplexes pages 1-2, galindo2021cryo‐emstructureof pages 9-10). The involvement of TRAPPIII in autophagy highlights the dual role of this complex in both biosynthetic (secretory) and catabolic (autophagic) membrane trafficking pathways.
Rab1 activation by TRAPPIII is necessary for maintaining the structural integrity of the Golgi apparatus (maeda2025disease‐associatedfactorsat pages 8-9). Studies have shown that depletion or inhibition of TRAPPC13 or other TRAPPIII components can lead to Golgi fragmentation and disruption of ER-Golgi transport, underscoring the importance of this complex in Golgi homeostasis (maeda2025disease‐associatedfactorsat pages 9-11, maeda2025disease‐associatedfactorsat pages 8-9).
The TRAPPIII complex, including TRAPPC13, is highly specific for Rab1 as its physiological GTPase substrate (galindo2023thetrappcomplexes pages 1-2, galindo2023thetrappcomplexes pages 2-3, galindo2021cryo‐emstructureof pages 1-2). This specificity is remarkable because TRAPPIII and TRAPPII share an identical catalytic core yet activate different Rab GTPases—Rab1 and Rab11, respectively (galindo2023thetrappcomplexes pages 1-2, galindo2023thetrappcomplexes pages 2-3, bagde2023thetrappcomplexes pages 1-3). Recent structural and biochemical studies have revealed that substrate specificity is determined by the large accessory subunits rather than the core (galindo2021cryo‐emstructureof pages 1-2, bagde2023thetrappcomplexes pages 1-3). The TRAPPC8 arm of TRAPPIII is positioned to contact Rab1 when it is bound to the catalytic core, thereby enhancing both the affinity and specificity of the interaction (galindo2021cryo‐emstructureof pages 7-9, galindo2021cryo‐emstructureof pages 9-10). The C-terminal hypervariable domain (HVD) of Rab1, which connects the GTPase domain to the membrane via prenyl anchors, also plays a role in substrate discrimination, with yeast studies showing that the length of the HVD is critical for preventing promiscuous activation by the wrong TRAPP complex (bagde2023thetrappcomplexes pages 3-5, bagde2023thetrappcomplexes pages 1-3).
Biochemical assays have confirmed that TRAPPIII has robust GEF activity toward Rab1 and can also activate Rab43 (a Rab1 family member), but shows no detectable activity toward Rab11 or most other Rab GTPases tested (galindo2021cryo‐emstructureof pages 1-2, bagde2023thetrappcomplexes pages 1-3). This stringent specificity ensures that Rab1 is activated only at appropriate membrane compartments where TRAPPIII is localized.
TRAPPC13 is relatively ubiquitously expressed across human tissues, consistent with the fundamental importance of membrane trafficking in all cell types (hall2024trappopathiesseveremultisystem pages 1-2). Despite this broad expression pattern, TRAPPC13 is reported to be non-essential for viability in human cell lines, in contrast to TRAPPC8 and TRAPPC11, which are essential for Rab1 recruitment and cell viability (hall2024trappopathiesseveremultisystem pages 4-5, galindo2023thetrappcomplexes pages 3-5, galindo2021cryo‐emstructureof pages 1-2). This differential essentiality suggests that while TRAPPC12 and TRAPPC13 contribute to the structural organization and potentially the regulation of TRAPPIII, they are not absolutely required for the minimal GEF activity necessary to sustain cellular function under standard culture conditions. However, they may play important regulatory or modulatory roles in vivo under physiological stress or in specific developmental contexts that have not yet been fully characterized.
To date, no monogenic human diseases have been specifically attributed to mutations in TRAPPC13 (hall2024trappopathiesseveremultisystem pages 1-2, hall2024trappopathiesseveremultisystem pages 2-4). This contrasts with several other TRAPP subunits, where pathogenic variants cause a spectrum of disorders collectively termed "TRAPPopathies," including neurodevelopmental disorders, muscular dystrophies, and skeletal dysplasias (hall2024trappopathiesseveremultisystem pages 1-2, hall2024trappopathiesseveremultisystem pages 2-4, hall2024trappopathiesseveremultisystem pages 4-5). For example, mutations in TRAPPC2 cause spondyloepiphyseal dysplasia tarda (SEDT), mutations in TRAPPC11 cause limb-girdle muscular dystrophy type 18 (LGMD18), and mutations in TRAPPC4 and TRAPPC6B cause severe neurodevelopmental disorders (hall2024trappopathiesseveremultisystem pages 2-4, hall2024trappopathiesseveremultisystem pages 4-5, maeda2025disease‐associatedfactorsat pages 9-11, maeda2025disease‐associatedfactorsat pages 8-9). The absence of reported disease associations for TRAPPC13 may reflect: (1) genuine functional redundancy or dispensability in humans, consistent with its non-essential status in cell lines; (2) the possibility that TRAPPC13 mutations are embryonic lethal and thus not observed in clinical populations; or (3) insufficient clinical genetic data, as TRAPPC13-related disorders may be extremely rare or yet to be identified.
Recent authoritative reviews have synthesized the growing understanding of TRAPP complex biology. Hall et al. (2024) provided a comprehensive review of TRAPPopathies, explicitly noting that TRAPPC13 has no reported disease associations despite being relatively ubiquitously expressed (hall2024trappopathiesseveremultisystem pages 1-2). Galindo and Munro (2023) published a detailed review in FEBS Letters summarizing the structural mechanisms by which TRAPP complexes discriminate between Rab substrates, integrating cryo-EM structures with functional data (galindo2023thetrappcomplexes pages 1-2, galindo2023thetrappcomplexes pages 2-3). Maeda et al. (2025) reviewed disease-associated factors at the ER-Golgi interface, discussing TRAPPC13 in the context of TRAPPIII's role in maintaining ER and Golgi homeostasis (maeda2025disease‐associatedfactorsat pages 1-2, maeda2025disease‐associatedfactorsat pages 8-9). These recent works emphasize that while structural details of TRAPPC13 are now well-defined, functional characterization—particularly regarding its regulatory roles in vivo—remains an area for future investigation.
While the structural position and general function of TRAPPC13 within TRAPPIII are now well-established, several important questions remain. First, the precise regulatory role of TRAPPC13 and TRAPPC12 at the vertex of TRAPPIII is unclear. Although they are dispensable for in vitro GEF activity, they may modulate GEF activity, membrane recruitment, or complex stability in response to cellular signals. Second, the lack of disease associations for TRAPPC13 mutations requires further investigation to determine whether this reflects true dispensability or whether mutations remain undiscovered. Third, the evolutionary origin and conservation of TRAPPC13 across species (present in metazoans but absent in budding yeast, which lacks TRAPPC11, TRAPPC12, and TRAPPC13) suggests that these subunits confer additional regulatory complexity in higher eukaryotes, but the nature of this regulation is poorly understood.
| Property | Description | Evidence/Citations |
|---|---|---|
| Gene name/synonyms | Human TRAPPC13 encodes trafficking protein particle complex subunit 13; the target identity is consistent with the human TRAPPIII-specific subunit discussed in structural and review literature. The user-provided synonym is C5orf44. | (hall2024trappopathiesseveremultisystem pages 1-2, galindo2021cryo‐emstructureof pages 1-2) |
| Protein complex membership | TRAPPC13 is a metazoan TRAPPIII-specific subunit. TRAPPIII in humans/metazoans comprises the shared TRAPP core plus TRAPPC8, TRAPPC11, TRAPPC12, and TRAPPC13. | (galindo2023thetrappcomplexes pages 2-3, hall2024trappopathiesseveremultisystem pages 4-5, maeda2025disease‐associatedfactorsat pages 8-9, galindo2021cryo‐emstructureof pages 1-2) |
| Structural role in complex | Cryo-EM places TRAPPC13, together with TRAPPC12, at the vertex/joint where the TRAPPC8 and TRAPPC11 arms meet, helping organize the triangular TRAPPIII architecture. TRAPPC13 is therefore best understood as a structural/accessory subunit rather than the catalytic GEF center. | (galindo2023thetrappcomplexes pages 5-7, galindo2021cryo‐emstructureof pages 1-2, galindo2021cryo‐emstructureof pages 10-12) |
| Subcellular localization | TRAPPC13 acts as part of TRAPPIII on membrane trafficking compartments of the early secretory pathway, especially the ER-Golgi interface / ERGIC / Golgi-associated membranes, and in autophagy-related membranes where Rab1 is activated. The exact localization evidence is mainly at the complex level rather than TRAPPC13 alone. | (galindo2023thetrappcomplexes pages 1-2, hall2024trappopathiesseveremultisystem pages 4-5, maeda2025disease‐associatedfactorsat pages 8-9, galindo2021cryo‐emstructureof pages 9-10) |
| Primary molecular function | TRAPPC13 does not itself catalyze nucleotide exchange; instead it contributes to the assembly/stability/organization of the TRAPPIII Rab1 GEF complex. Through TRAPPIII, it supports activation of Rab1 by promoting the complex architecture needed for membrane trafficking and autophagy in vivo. | (galindo2023thetrappcomplexes pages 1-2, galindo2021cryo‐emstructureof pages 1-2, galindo2021cryo‐emstructureof pages 9-10, bagde2023thetrappcomplexes pages 1-3) |
| Biological processes | By virtue of its role in TRAPPIII, TRAPPC13 is implicated in ER-to-Golgi transport, early secretory pathway organization, Golgi homeostasis, and autophagosome formation/autophagy. | (hall2024trappopathiesseveremultisystem pages 1-2, galindo2023thetrappcomplexes pages 1-2, hall2024trappopathiesseveremultisystem pages 4-5, maeda2025disease‐associatedfactorsat pages 8-9, bagde2023thetrappcomplexes pages 1-3) |
| Substrate specificity | TRAPPC13 has no independent substrate specificity known. At the complex level, TRAPPIII is the physiological GEF for Rab1 in metazoans; Rab1 is the relevant small GTPase substrate for the TRAPPC13-containing complex. | (galindo2023thetrappcomplexes pages 1-2, galindo2023thetrappcomplexes pages 2-3, galindo2021cryo‐emstructureof pages 1-2, bagde2023thetrappcomplexes pages 1-3) |
| Essential for viability | Recent reviews summarize TRAPPC13 as non-essential for viability in human cell lines, in contrast to TRAPPC8 and TRAPPC11, which are reported as essential for Rab1 recruitment/activity in vivo. Consistent with this, TRAPPIII lacking TRAPPC12/TRAPPC13 retained Rab1 GEF activity in vitro in a recombinant “miniTRAPPIII” preparation. | (galindo2023thetrappcomplexes pages 3-5, galindo2021cryo‐emstructureof pages 1-2) |
| Disease associations | As of recent reviews, there are no specific monogenic human disease associations reported for TRAPPC13, unlike several other TRAPP subunits. Reviews of TRAPPopathies explicitly note no reported disease associations for TRAPPC13. | (hall2024trappopathiesseveremultisystem pages 2-4, hall2024trappopathiesseveremultisystem pages 1-2) |
| Tissue expression pattern | TRAPPC13 is reported to be relatively ubiquitously expressed across human tissues, with some tissues showing higher expression than others; however, recent reviews emphasize that detailed functional and disease data remain limited. | (hall2024trappopathiesseveremultisystem pages 1-2) |
Table: This table summarizes the best-supported structural and functional features of human TRAPPC13 based on recent TRAPP-complex literature. It highlights what is established directly from cryo-EM and biochemical studies, while distinguishing areas where evidence is still limited or inferential.
TRAPPC13 (C5orf44, UniProt A5PLN9) is a structural component of the metazoan TRAPPIII complex that functions at the ER-Golgi interface and during autophagy to support Rab1 activation. Together with TRAPPC12, TRAPPC13 occupies a vertex position at the junction between the TRAPPC8 and TRAPPC11 arms of the triangular TRAPPIII architecture, contributing to complex organization and stability. While not directly involved in catalysis and non-essential for basal GEF activity in vitro, TRAPPC13 is part of a sophisticated molecular machine that ensures precise spatiotemporal activation of Rab1, a master regulator of ER-to-Golgi transport, Golgi homeostasis, and autophagosome formation. The absence of reported disease associations for TRAPPC13, in contrast to other TRAPP subunits, suggests either functional redundancy or yet-to-be-discovered clinical relevance. Ongoing research, particularly utilizing recent high-resolution structural insights from cryo-EM studies (2021-2023) and comprehensive reviews (2023-2025), continues to refine our understanding of how TRAPPC13 and the TRAPPIII complex orchestrate membrane trafficking in human cells.
References
(hall2024trappopathiesseveremultisystem pages 1-2): Riley Hall, Vallari Sawant, Jinchao Gu, Tim Sikora, Ben Rollo, Silvia Velasco, Jinkuk Kim, Nava Segev, John Christodoulou, and Nicole J. Van Bergen. Trappopathies: severe multisystem disorders caused by variants in genes of the transport protein particle (trapp) complexes. International Journal of Molecular Sciences, 25:13329, Dec 2024. URL: https://doi.org/10.3390/ijms252413329, doi:10.3390/ijms252413329. This article has 8 citations.
(galindo2021cryo‐emstructureof pages 1-2): Antonio Galindo, Vicente J Planelles‐Herrero, Gianluca Degliesposti, and Sean Munro. Cryo‐em structure of metazoan trappiii, the multi‐subunit complex that activates the gtpase rab1. The EMBO Journal, May 2021. URL: https://doi.org/10.15252/embj.2020107608, doi:10.15252/embj.2020107608. This article has 49 citations.
(galindo2023thetrappcomplexes pages 2-3): Antonio Galindo and Sean Munro. The
(hall2024trappopathiesseveremultisystem pages 4-5): Riley Hall, Vallari Sawant, Jinchao Gu, Tim Sikora, Ben Rollo, Silvia Velasco, Jinkuk Kim, Nava Segev, John Christodoulou, and Nicole J. Van Bergen. Trappopathies: severe multisystem disorders caused by variants in genes of the transport protein particle (trapp) complexes. International Journal of Molecular Sciences, 25:13329, Dec 2024. URL: https://doi.org/10.3390/ijms252413329, doi:10.3390/ijms252413329. This article has 8 citations.
(galindo2023thetrappcomplexes pages 1-2): Antonio Galindo and Sean Munro. The
(galindo2021cryo‐emstructureof pages 3-4): Antonio Galindo, Vicente J Planelles‐Herrero, Gianluca Degliesposti, and Sean Munro. Cryo‐em structure of metazoan trappiii, the multi‐subunit complex that activates the gtpase rab1. The EMBO Journal, May 2021. URL: https://doi.org/10.15252/embj.2020107608, doi:10.15252/embj.2020107608. This article has 49 citations.
(galindo2021cryo‐emstructureof pages 7-9): Antonio Galindo, Vicente J Planelles‐Herrero, Gianluca Degliesposti, and Sean Munro. Cryo‐em structure of metazoan trappiii, the multi‐subunit complex that activates the gtpase rab1. The EMBO Journal, May 2021. URL: https://doi.org/10.15252/embj.2020107608, doi:10.15252/embj.2020107608. This article has 49 citations.
(galindo2023thetrappcomplexes pages 5-7): Antonio Galindo and Sean Munro. The
(galindo2021cryo‐emstructureof pages 5-7): Antonio Galindo, Vicente J Planelles‐Herrero, Gianluca Degliesposti, and Sean Munro. Cryo‐em structure of metazoan trappiii, the multi‐subunit complex that activates the gtpase rab1. The EMBO Journal, May 2021. URL: https://doi.org/10.15252/embj.2020107608, doi:10.15252/embj.2020107608. This article has 49 citations.
(bagde2023thetrappcomplexes pages 1-3): Saket R. Bagde and J. Christopher Fromme. The
(galindo2021cryo‐emstructureof pages 9-10): Antonio Galindo, Vicente J Planelles‐Herrero, Gianluca Degliesposti, and Sean Munro. Cryo‐em structure of metazoan trappiii, the multi‐subunit complex that activates the gtpase rab1. The EMBO Journal, May 2021. URL: https://doi.org/10.15252/embj.2020107608, doi:10.15252/embj.2020107608. This article has 49 citations.
(maeda2025disease‐associatedfactorsat pages 8-9): Miharu Maeda, Masashi Arakawa, and Kota Saito. Disease‐associated factors at the endoplasmic reticulum–golgi interface. Traffic (Copenhagen, Denmark), Jan 2025. URL: https://doi.org/10.1111/tra.70001, doi:10.1111/tra.70001. This article has 2 citations.
(maeda2025disease‐associatedfactorsat pages 1-2): Miharu Maeda, Masashi Arakawa, and Kota Saito. Disease‐associated factors at the endoplasmic reticulum–golgi interface. Traffic (Copenhagen, Denmark), Jan 2025. URL: https://doi.org/10.1111/tra.70001, doi:10.1111/tra.70001. This article has 2 citations.
(papaioannou2023biochemicalstructureand pages 1-2): Peter Papaioannou, Michael J. Wallace, Nipun Malhotra, Peter J. Mohler, and Mona El Refaey. Biochemical structure and function of trapp complexes in the cardiac system. Dec 2023. URL: https://doi.org/10.1016/j.jacbts.2023.03.011, doi:10.1016/j.jacbts.2023.03.011. This article has 11 citations.
(galindo2021cryo‐emstructureof pages 10-12): Antonio Galindo, Vicente J Planelles‐Herrero, Gianluca Degliesposti, and Sean Munro. Cryo‐em structure of metazoan trappiii, the multi‐subunit complex that activates the gtpase rab1. The EMBO Journal, May 2021. URL: https://doi.org/10.15252/embj.2020107608, doi:10.15252/embj.2020107608. This article has 49 citations.
(maeda2025disease‐associatedfactorsat pages 9-11): Miharu Maeda, Masashi Arakawa, and Kota Saito. Disease‐associated factors at the endoplasmic reticulum–golgi interface. Traffic (Copenhagen, Denmark), Jan 2025. URL: https://doi.org/10.1111/tra.70001, doi:10.1111/tra.70001. This article has 2 citations.
(bagde2023thetrappcomplexes pages 3-5): Saket R. Bagde and J. Christopher Fromme. The
(galindo2023thetrappcomplexes pages 3-5): Antonio Galindo and Sean Munro. The
(hall2024trappopathiesseveremultisystem pages 2-4): Riley Hall, Vallari Sawant, Jinchao Gu, Tim Sikora, Ben Rollo, Silvia Velasco, Jinkuk Kim, Nava Segev, John Christodoulou, and Nicole J. Van Bergen. Trappopathies: severe multisystem disorders caused by variants in genes of the transport protein particle (trapp) complexes. International Journal of Molecular Sciences, 25:13329, Dec 2024. URL: https://doi.org/10.3390/ijms252413329, doi:10.3390/ijms252413329. This article has 8 citations.