TRPC4AP Membrane Protein Introduction

Introduction of TRPC4AP

Transient receptor potential cation channel subfamily C member 4 associated protein (TRPC4AP), also known as protein TAP1, TNF-receptor ubiquitous scaffolding/signaling protein, is encoded by human gene TRPC4AP. The entire N-terminal region (AAs 1-440) of TRPC4AP is involved in its interaction with TNFRSF1A and within this region. AAs 249-440 play an important role in the interaction with TRAF2. The C-terminal region of TRPC4AP may contribute to its oligomerization. TRPC4AP has a ubiquitous expression in placenta, spleen, adrenal, appendix, bone marrow, brain, lung, and 20 other tissues. There are two putative TRAF2 binding sites, several putative Ser/Thr and Tyr kinase phosphorylation sites have been found for TRPC4AP.

Basic Information of TRPC4AP
Protein Name	Short transient receptor potential channel 4-associated protein
Gene Name	TRPC4AP
Aliases	Protein TAP1, TNF-receptor ubiquitous scaffolding/signaling protein, TRUSS
Organism	Homo sapiens (Human)
UniProt ID	Q8TEL6
Transmembrane Times
Length (aa)	797
Sequence	MAAAPVAAGSGAGRGRRSAATVAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKQSKWSGIPQLLLKLHTTSHLHSDFVECQNILKEISPLLSMEAMAFVTEERKLTQETTYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQELEEWYTWLDNALVLDALMRVANEESEHNQASIVFPPPGASEENGLPHTSARTQLPQSMKIMHEIMYKLEVLYVLCVLLMGRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQELNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGLLEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFENQVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKKYPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE

Function of TRPC4AP Membrane Protein

TRPC4AP, also known as TRUSS, is a substrate-specific adapter of a DDB1-CUL4-X-box (DCX) E3 ubiquitin-protein ligase complex, which is essential for cell cycle control. The DDB1-CUL4-X-box complex specifically regulates the polyubiquitination of MYC and subsequently leads to the degradation of it. TRPC4AP also plays a role in the activation of NFKB1 in response to ligation of TNFRSF1A, probably by linking TNFRSF1A to the IKK signalosome. Additionally, it is thought to be involved in the elevation of endoplasmic reticulum Ca²⁺ storage reduction in response to muscarinic acetylcholine receptor M₁ and involved in c-Jun N-terminal kinases activation via its interaction with TRAF2. The subcellular location of TRPC4AP is the plasma membrane.

Fig.1 Schematic representation of a simulated TRPC4AP structure provided by MODBASE. (Ursula, 2014)

Application of TRPC4AP Membrane Protein in Literature

Poduslo S.E., et al. The frequency of the TRPC4AP haplotype in Alzheimer's patients. Neurosci Lett. 2009, 450(3):344-6. PubMed ID: 19059308

This article suggests that the patients with this TRPC4AP haplotype may have more hallucinations and more behavioral changes when clinical phenotypes are analyzed.
Poduslo S.E., et al. Genome screen of late-onset Alzheimer's extended pedigrees identifies TRPC4AP by haplotype analysis. Am J Med Genet B Neuropsychiatr Genet. 2009, 150B(1):50-5. PubMed ID: 18449908

This article suggests that TRPC4AP is associated with the disease in these late-onset Alzheimer's families.
Choi S.H., et al. Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells. Genes Dev. 2010, 24(12):1236-41. PubMed ID: 20551172

This article finds that the expression of TRPC4AP is significantly down-regulated in most cancer cell lines, leading to stabilization of Myc protein.
Jamal A., et al. The G1 phase E3 ubiquitin ligase TRUSS that gets deregulated in human cancers is a novel substrate of the S-phase E3 ubiquitin ligase Skp2. Cell Cycle. 2015, 14(16):2688-700. PubMed ID: 26038816

This report suggests that TRUSS is a novel substrate of E3 ligase Skp2 and demonstrates that interruption of Skp2-TRUSS interaction by viral oncoproteins could cause pathophysiological sequelae.
Terry Powers J.L., et al. TNF receptor-1 (TNF-R1) ubiquitous scaffolding and signaling protein interacts with TNF-R1 and TRAF2 via an N-terminal docking interface. Biochemistry. 2010, 49(36):7821-9. PubMed ID: 20704259

This article demonstrates that the assembly of homomeric TRUSS complexes may play a role in TNF-R1 signaling.

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Reference

Ursula Pieper, et al. (2014). MODBASE, a database of annotated comparative protein structure models and associated resources. Acids Research. 42: D336-46.

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