TY - CHAP
T1 - The small heat-shock proteins
T2 - Cellular functions and mutations causing neurodegeneration
AU - D'Ydewalle, C.
AU - Krishnan, J.
AU - Timmerman, V.
AU - Van Den Bosch, L.
N1 - Publisher Copyright:
© Springer Science+Business Media, LLC 2011. All rights reserved.
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2011
Y1 - 2011
N2 - Small heat-shock proteins (small Hsps) are a family of highly-conserved proteins involved in multiple cellular mechanisms. Apart from their central role as chaperones in protecting cells during stressful conditions (as outlined in the previous-two chapters), small Hsps also function to maintain-cellular homeostasis-in physiological conditions. Correct protein refolding to avoid aggregation, -targeting misfolded proteins for degradation, proper cytoskeletal organization, and anti-apoptotic functions are some of the extensively studied attributes of small Hsps. One or more of these cellular mechanisms may malfunction in -specific sets of neurons leading to neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, polyglutamine disorders, and amyotrophic lateral sclerosis. Many in vitro models of these diseases have demonstrated the beneficial roles of small Hsps pointing out their protective role in attenuating the neurodegenerative phenotype. Interestingly, mutations in small Hsps themselves were linked to other degenerative disorders like inherited peripheral neuropathies and familial myopathies. Although not much is known regarding the exact patho-mechanism (loss of function or gain of function) of mutations in causing disease, these discoveries reiterate the importance of small Hsps in maintaining neuronal health and indicate that the small Hsp family of proteins might have more functions than meets the eye. This chapter reviews the current knowledge regarding these enigmatic proteins, including their structure and function and how mutations in these once forgotten proteins might alter their functions and cause neurodegeneration.
AB - Small heat-shock proteins (small Hsps) are a family of highly-conserved proteins involved in multiple cellular mechanisms. Apart from their central role as chaperones in protecting cells during stressful conditions (as outlined in the previous-two chapters), small Hsps also function to maintain-cellular homeostasis-in physiological conditions. Correct protein refolding to avoid aggregation, -targeting misfolded proteins for degradation, proper cytoskeletal organization, and anti-apoptotic functions are some of the extensively studied attributes of small Hsps. One or more of these cellular mechanisms may malfunction in -specific sets of neurons leading to neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, polyglutamine disorders, and amyotrophic lateral sclerosis. Many in vitro models of these diseases have demonstrated the beneficial roles of small Hsps pointing out their protective role in attenuating the neurodegenerative phenotype. Interestingly, mutations in small Hsps themselves were linked to other degenerative disorders like inherited peripheral neuropathies and familial myopathies. Although not much is known regarding the exact patho-mechanism (loss of function or gain of function) of mutations in causing disease, these discoveries reiterate the importance of small Hsps in maintaining neuronal health and indicate that the small Hsp family of proteins might have more functions than meets the eye. This chapter reviews the current knowledge regarding these enigmatic proteins, including their structure and function and how mutations in these once forgotten proteins might alter their functions and cause neurodegeneration.
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U2 - 10.1007/978-1-4419-7061-9_4
DO - 10.1007/978-1-4419-7061-9_4
M3 - Chapter
AN - SCOPUS:80052486651
SN - 9781441970602
VL - 9781441970619
SP - 49
EP - 77
BT - Folding for the synapse
PB - Springer US
ER -