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Cited by 8Drug Transport and Resistance MechanismsProtein Kinase Regulation and GTPase SignalingGlutathione Transferases and Polymorphisms

RLIP76: A Structural and Functional Triumvirate

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Cornish, Jasmine, Owen, Darerca, Mott, Helen R.·2021·Cancers
DOI 10.3390/cancers13092206PMC PMC8124665
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Abstract

RLIP76/RalBP1 is an ATP-dependent transporter of glutathione conjugates, which is overexpressed in various human cancers, but its diverse functions in normal cells, which include endocytosis, stress response and mitochondrial dynamics, are still not fully understood. The protein can be divided into three distinct regions, each with its own structural properties. At the centre of the protein are two well-defined domains, a GTPase activating protein domain targeting Rho family small G proteins and a small coiled-coil that binds to the Ras family small GTPases RalA and RalB. In engaging with Rho and Ral proteins, RLIP76 bridges these two distinct G protein families. The N-terminal region is predicted to be disordered and is rich in basic amino acids, which may mediate membrane association, consistent with its role in transport. RLIP76 is an ATP-dependent transporter with ATP-binding sites within the N-terminus and the Ral binding domain. Furthermore, RLIP76 is subject to extensive phosphorylation, particularly in the N-terminal region. In contrast, the C-terminal region is thought to form an extensive coiled-coil that could mediate dimerization. Here, we review the structural features of RLIP76, including experimental data and computational predictions, and discuss the implications of its various post-translational modifications.

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  • Reps1, Ralbp1, and RalA are all implicated in a range of physiological and pathological processes.

    “Reps1, Ralbp1, and RalA are all implicated in a range of physiological and pathological processes (10, 61, 62).”

    From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [62]

    The Introduction identifies RalBP1 as RLIP76, links Ral proteins to cell growth and metastasis, and describes RLIP76’s involvement in multiple cancers. Section 2 identifies REPS1 as an RLIP76-interacting protein involved in receptor-mediated endocytosis, but the paper does not establish a range of pathological processes involving REPS1. Thus it supports the broad statement for RalA and RalBP1, but not fully for all three proteins. (LLM, conf=0.83)

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Cited by

Sorted by citations

Authors
Cornish, J., Owen, D., & Mott, H. R.
Affiliations
University of Cambridge (GB)
Corresponding author
Mott, Helen R.
ORCID
Venue
Cancers
Publisher
MDPI AG
Published
2021-05-04
Volume
13
Issue
9
Pages
2206
ISSN
2072-6694 (ISSN-L)
DOI
10.3390/cancers13092206
PMC
PMC8124665
OpenAlex
W3157549653
Cited by
8
References
4
Citations by year
2026: 1 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 3
FWCI
0.18
Type
journal article
Language
en
Open access
Licence
Locations
  • Cancers (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Apollo (University of Cambridge) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Apollo
  • Apollo (cc-by)
Topics
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords
RLIP76, RALBP1, glutathione conjugate transport, Rho GTPases, Ral GTPase, coiled coil, protein structure, phosphorylation, post-translational modification, cancer overexpression, mitochondrial dynamics, endocytosis, stress response

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