Assistance for Folding of Disease-Causing Plasma Membrane Proteins

Juarez-Navarro, Karina; Ayala‐García, Víctor M.; Ruiz-Baca, Estela; Meneses-Morales, Iván; Rios-Banuelos, Jose Luis; Lopez-Rodriguez, Angélica

doi:10.3390/biom10050728

Cited by 3 publications

(3 citation statements)

References 338 publications

(351 reference statements)

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“…The capacity of molecular chaperone proteins to recognize and interact with the client protein's exposed hydrophobic regions allows them to perform these diverse functions. These interactions prevent erroneous protein association or aggregation and guide proteins through folding, transport, or degradation pathways [18].…”

Section: Background On Hsps As Molecular Chaperones Proteinsmentioning

confidence: 99%

Implications of sperm heat shock protein 70-2 in bull fertility

et al. 2022

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Heat shock protein 70 (HSP70) is one of the most abundant chaperone proteins. Their function is well documented in facilitating the protein synthesis, translocation, de novo folding, and ordering of multiprotein complexes. HSP70 in bovine consists of four genes: HSP70-1, HSP70-2, HSP70-3, and HSP70-4. HSP70-2 was found to be involved in fertility. Current knowledge implicates HSP70-2 in sperm quality, sperm capacitation, sperm–egg recognition, and fertilization essential for bull reproduction. HSP70-2 is also involved in the biological processes of spermatogenesis, as it protects cells from the effects of apoptosis and oxidative stress. Fertilization success is not only determined by the amount of sperm found in the female reproductive tract but also by the functional ability of the sperm. However, subfertility is more likely to be associated with changes in sperm molecular dynamics not detectable using conventional methods. As such, molecular analyses and omics methods have been developed to monitor crucial aspects of sperm molecular morphology that are important for sperm functions, which are the objectives of this review.

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Section: Background On Hsps As Molecular Chaperones Proteinsmentioning

confidence: 99%

Implications of sperm heat shock protein 70-2 in bull fertility

et al. 2022

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“…Hence, the biogenesis, trafficking, stability, and degradation of PM proteins are far more challenging than soluble cytosolic proteins. Cells are extremely sensitive to conformationally compromised PM proteins, and often this leads to loss of cell integrity or death ( Zhao et al, 2013 ; Juarez-Navarro et al, 2020 ). To circumvent this, cells employ efficient, multi-layered cellular protein quality control (PQC) machineries which act as stringent checkpoints to tightly regulate the synthesis, folding, and degradation of PM proteins (Reviewed in ( Apaja et al, 2010 ; Okiyoneda et al, 2011 ; Babst, 2014 ; MacGurn, 2014 ; Sardana and Emr, 2021 ; Vasconcelos-Cardoso et al, 2022 ).…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, the ability of selected Hsp70s and JDPs to directly associate with lipids and membranes sheds light on their possible role in the PM as well ( Caplan et al, 1992 ; Kanazawa et al, 1997 ; Beilharz et al, 2003 ; Kalli et al, 2013 ; Radons, 2016 ; Sopha et al, 2017 ; Sjögren et al, 2018 ; Dobriyal et al, 2020 ; De Maio and Hightower, 2021 ; Zhang et al, 2021 ) ( Table 1 ). The importance of different chaperones and other PQC factors in diseases associated with PM proteins is discussed elsewhere ( Juarez-Navarro et al, 2020 ). In this review, we collate data available from multiple organisms, including yeast, plants, and mammalian models, and come up with a unifying model to show that, like cytosolic proteins, the versatile Hsp70:JDP systems are guardians of PM proteins as well, throughout their odyssey in the cell ( Table 2 ).…”

Section: Introductionmentioning

confidence: 99%

Volleying plasma membrane proteins from birth to death: Role of J-domain proteins

Sagarika

Yadav

Sahi

2022

Front. Mol. Biosci.

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The function, stability, and turnover of plasma membrane (PM) proteins are crucial for cellular homeostasis. Compared to soluble proteins, quality control of plasma membrane proteins is extremely challenging. Failure to meet the high quality control standards is detrimental to cellular and organismal health. J-domain proteins (JDPs) are among the most diverse group of chaperones that collaborate with other chaperones and protein degradation machinery to oversee cellular protein quality control (PQC). Although fragmented, the available literature from different models, including yeast, mammals, and plants, suggests that JDPs assist PM proteins with their synthesis, folding, and trafficking to their destination as well as their degradation, either through endocytic or proteasomal degradation pathways. Moreover, some JDPs interact directly with the membrane to regulate the stability and/or functionality of proteins at the PM. The deconvoluted picture emerging is that PM proteins are relayed from one JDP to another throughout their life cycle, further underscoring the versatility of the Hsp70:JDP machinery in the cell.

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Cellular and molecular mechanisms underlying plasma membrane functionality and integrity

Vasconcelos-Cardoso

Batista-Almeida

Rios-Barros

et al. 2022

Journal of Cell Science

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The plasma membrane not only protects the cell from the extracellular environment, acting as a selective barrier, but also regulates cellular events that originate at the cell surface, playing a key role in various biological processes that are essential for the preservation of cell homeostasis. Therefore, elucidation of the mechanisms involved in the maintenance of plasma membrane integrity and functionality is of utmost importance. Cells have developed mechanisms to ensure the quality of proteins that inhabit the cell surface, as well as strategies to cope with injuries inflicted to the plasma membrane. Defects in these mechanisms can lead to the development or onset of several diseases. Despite the importance of these processes, a comprehensive and holistic perspective of plasma membrane quality control is still lacking. To tackle this gap, in this Review, we provide a thorough overview of the mechanisms underlying the identification and targeting of membrane proteins that are to be removed from the cell surface, as well as the membrane repair mechanisms triggered in both physiological and pathological conditions. A better understanding of the mechanisms underlying protein quality control at the plasma membrane can reveal promising and unanticipated targets for the development of innovative therapeutic approaches.

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Assistance for Folding of Disease-Causing Plasma Membrane Proteins

Cited by 3 publications

References 338 publications

Implications of sperm heat shock protein 70-2 in bull fertility

Implications of sperm heat shock protein 70-2 in bull fertility

Volleying plasma membrane proteins from birth to death: Role of J-domain proteins

Cellular and molecular mechanisms underlying plasma membrane functionality and integrity

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