Published online Sep 27, 2021. doi: 10.4331/wjbc.v12.i5.70
Peer-review started: March 31, 2021
First decision: June 7, 2021
Revised: June 21, 2021
Accepted: August 3, 2021
Article in press: August 3, 2021
Published online: September 27, 2021
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The prevalence of type 2 diabetes (T2D) continues to rise despite the amount of research dedicated to finding the culprits of this debilitating disease. Skeletal muscle is arguably the most important contributor to glucose disposal making it a clear target in insulin resistance and T2D research. Within skeletal muscle there is a clear link to metabolic dysregulation during the progression of T2D but the determination of culprits vs consequences of the disease has been elusive. Emerging evidence in skeletal muscle implicates influential cross talk between a key anabolic regulatory protein, the mammalian target of rapamycin (mTOR) and its associated complexes (mTORC1 and mTORC2), and the well-described cano
Core Tip: The prevalence of type 2 diabetes (T2D) continues to rise despite the amount of research dedicated to finding the culprits of this debilitating disease. Within skeletal muscle there is a clear link to metabolic dysregulation during the progression of T2D but the determination of culprits vs consequences of the disease has been elusive. Emerging evidence in skeletal muscle implicates influential cross talk between the mammalian target of rapamycin (mTOR) complexes (mTORC1 and mTORC2) during insulin stimulated glucose uptake. This review highlights interactions between protein and glucose regulatory pathways and the implications this may have for the control of glucoregulatory function in skeletal muscle.
- Citation: O'Reilly CL, Uranga S, Fluckey JD. Culprits or consequences: Understanding the metabolic dysregulation of muscle in diabetes. World J Biol Chem 2021; 12(5): 70-86
- URL: https://www.wjgnet.com/1949-8454/full/v12/i5/70.htm
- DOI: https://dx.doi.org/10.4331/wjbc.v12.i5.70
Globally, 462 million individuals are affected by type 2 diabetes (T2D) and it is ranked as the 9th leading cause of mortality[1]. The prevalence of diabetes over the past few decades has continued to rise with no sign of this changing[1]. T2D is characterized by insulin resistance and hyperglycemia and can lead to various other outcomes and comorbidities reducing quality of life in those effected. While the pathogenesis and progression of T2D is still widely debated, it is clear that a complex interplay between the pancreas and peripheral tissues is dependent for maintenance of glucose homeo
The insulin signaling cascade involves both glucoregulatory and anabolic processes which is outlined in Figure 1. Insulin responsive tissues have insulin receptors (IR) on the cell surface plasma membrane. These IR contain subunits where insulin can bind as well as residues that provide docking sites for downstream signaling molecules including the IR substrates (IRS). The two predominant insulin receptor substrates are IRS1 and IRS2 with similar sequences but specific signaling roles[8,9]. IRS1 appears to be the insulin receptor substrate protein whose primary responsibility is glucose re
This serine/threonine kinase is part of the AGC protein family and is known for its diverse function in growth, survival, proliferation and most importantly substrate metabolism[11-13] AKT is often referred to as one molecule but actually comprises of three distinct isoforms (AKT1, AKT2, AKT3) , while all isoforms are present in skeletal muscle, AKT2 is the most prevalent[12], but varies from low to immeasurable amounts in skeletal muscle[14,15]. While defining the variation and overlap between the AKT isoforms is important and needed, it is beyond the scope of this review but what is known currently can be found in these reviews[12,16] It is important to note that AKT2 is expressed primarily in insulin responsive tissues like fat and skeletal muscle and is the most abundant isoform in skeletal muscle[14,15,17,18]. AKT is as a critical regula
The upstream regulation of AKT, in its most simple iteration, appears to be very similar across isoforms. The two common phosphorylation sites of AKT are Ser473 (Ser474 in AKT2) and Thr308. The insulin receptors IRS1 and IRS2 will activate the PI3K-dependent conversion of PIP2 to PIP3, and PIP3 will recruit Pyruvate Dehydrogenase Kinase 1 (PDK1) and AKT to the membrane where colocalization will allow for phosphorylation at the Thr308 by PDK1[12,13]. Further, some evidence suggests that mitogen-activated protein kinase-associated protein 1 (mSin1) of the mTORC2 comp
The regulation of mTORC2 activity by mSin1 phosphorylation is controversial. It has been proposed that PIP3) promotes mTORC2 activity directly[21,22]. Recent work has indicated a positive feedback loop between AKT and mTORC2 via phosphory
There is also considerable debate over what the phosphorylation of specific AKT sites implicates for AKT activity and substrate specificity. Much of the early work in AKT reported a requirement of phosphorylation at Ser473 for full activation[25-28]. However, more recent work in platelets[29], HEK cells[27,30], and skeletal muscle[31,32] demonstrated that not all downstream substrates are impacted by Ser473 phos
The implications of Ser473 phosphorylation via mTORC2 has been studied in various tissues. In mSin1 knockout mouse embryonic fibroblasts, a regulator of mTORC2 complex formation and stability, Forkhead box 01/03 (FOX01/3a) phospho
As previously mentioned AKT has various downstream substrates that make the action of this kinase quite diverse in cell function. These substrates include members of the mTOR complexes Pras40 and Sin1, Glucose uptake proteins AS160 and GSK-3, Protein synthesis related Tuberous sclerosis 2, and apoptotic signaling through the FOX0 family. This section will focus on signal transduction related to glucose uptake.
GLUT-4 is the predominant isoform of the GLUT family found in skeletal muscle, and one of insulin’s primary metabolic roles is to promote the translocation of GLUT-4 to the surface membrane. AKT has been linked to downstream substrates that impact insulin-dependent GLUT-4 translocation including GSK-3[41] as well as AKT Subs
AKT phosphorylates TSC2 at Thr1462 which regulates the tuberin-hamartin complex and it’s activity[51-53]. Phosphorylation at this site releases the tuberin-hamartin complex inhibition of the mTORC1 complex and allows for downstream targets to be phosphorylated[51]. mTORC1 is a prolific kinase with multiple downstream sub
It is generally agreed that glucose transport is the rate limiting step of glucose uptake, and the step most impacted by the progression of T2D. The consensus in diabetes research at large is that the translocation or trafficking of glucose transport molecules in skeletal muscle is impaired in T2D[43,62] but the culprit behind this impairment is still widely debated. In skeletal muscle GLUT-4 is the predominantly expressed isoform[63,64] and the localization of GLUT-4 has been confirmed with insulin[65], exercise[65,66] and hypoxia[67]. The first important finding with diabetes is that the limitation in glucose transport cannot be explained by production or maintenance of the GLUT itself, because total GLUT-4 protein is largely unchanged with diabetes[68-70]. This implies that the issue is not related to GLUT-4 expression, per se, but within the signaling cascades that assist in the translocation of GLUT-4 to the surface mem
As the initial step in the insulin signaling cascade, the insulin receptor was a primary target of research related to the breakdown of the glucoregulatory signals. While current data are conflicting on IR activity with some reporting impairment[62,71,72] and others reporting normal activity[73-77], it appears that the important signaling ‘defects’ of T2D are further down the signal cascade. Signaling defects in IRS1 phosphorylation[73,77-79] and PI3K[73,77,78,80,81], activity are consistently found in the diabetic model. More controversial is the activity of AKT with studies reporting significant reductions of insulin stimulated AKT phosphorylation on Ser473 or Thr308[69,75,82,83]. While others report not impact of T2D on insulin dependent phosphorylation[80,81]. Downstream substrates of AKT have also been presented in the diabetic model with reduced glycogen synthase activity with protein levels of GSK-3 reported as being elevated which would inhibit GS activity[84]. Additionally, insulin dependent phosphorylation of AS160 has also been reported to be higher in T2D[42], despite the fact that AKT phosphorylation was not different in the same study.
Despite the continued exploration and detailed understanding of what the signaling cascades are doing during diabetes, there is still no consensus on where these dys
It is well documented that muscle mass and strength decline with T2D[85,86] and contribute to a decline in quality life over time. Interestingly despite a loss in muscle mass, there appears to be an upregulation of protein synthesis and the anabolic signal cascade in diabetic muscle[87,88]. Previously, studies assessing anabolic responses [fractional synthesis rate (FSR)] in diabetic skeletal muscle have been inconsistent, ranging from decreased[89,90], to normal[91,92] but more recently increased FSR has been confirmed by our lab[87,88,93,94] and others[95,96]. In Fatty Zucker rats, a well-documented model for T2D, upregulated protein synthesis in specific muscle fractions and increased phosphorylation of S6K1 were observed despite an overall decrease in muscle mass. This upregulation of S6K1 appears to be linked to a loss of control of upstream mTOR activation. While the hyperactive mTOR activity may be a result of the maintained state of hyperinsulinemia with glucose intolerance, we suspect some
Our recent studies have demonstrated that the constitutive activation of mTOR may be a result of suppressed DEPTOR expression in the diabetic state. DEPTOR is one of the mTOR associated binding partners that can be a part of either mTORC1 or mTORC2 and is a negative regulator of mTOR activity. Similar to several lines of cancer[97]. DEPTOR is substantially lower in obese subjects[87,88]. Since DEPTOR is still a fairly new discovery in the mTOR signaling cascade, the implications of low DEPTOR and the regulation of mTORC1 are still speculative but the low DEPTOR appears to allow the downstream anabolic signals to go unchecked[98] which has implications for mRNA translation[99], as well as glucoregulatory signaling cascades. This is unbridled mTORC1 activity without concomitant muscle mass accretion is indicative of high protein turnover[88], where it may not be warranted or wanted. It is also an important bridge between mTORC1 and mTORC2 which will be discussed in a later section.
A relatively recent but important discovery in the connection of anabolic and glucoregulatory signaling paths is an inhibitory pathway that directly links S6K1 to IRS1. IRS1 can be serine phosphorylated through many pathways including c-Jun NH2-terminal kinase, IkB kinase, PKC, and S6K1[100,101]. It is now known that the insulin receptor contains multiple phosphorylation sites[102] and even in a basal state it is highly phosphorylated[103]. Ser/Thr phosphorylation of IRS-1 has been linked to the de
While we are gaining perspective in the current literature about the interaction between mTORC1 signaling for protein synthesis and the disruption of insulin sig
The mTORC2 complex is best known for its involvement in cell survival but is known to phosphorylate AKT through Ser473[25,114-117] as well as the PKC family[40,116-119]. This complex is composed of binding partners mSin1, DEPTOR, Protor1, mLST8 and RICTOR. While all of these binding partners play roles in mTORC2 ac
Work by others indicated that the muscle-specific deletion of RICTOR led to de
Exercise and physical activity are effective, low cost interventions for insulin resistance and T2D[126,127]. The benefits of aerobic exercise on glucose tolerance are well es
It is often speculated that insulin-resistant skeletal muscle is desensitized or ‘re
Aside from insulin sensitivity, there are benefits to regular exercise, whether it is of an aerobic or anaerobic nature. It is important to note here that there are insulin independent pathways that trigger glucose uptake that are directly related to skeletal muscle contraction. This pathway is triggered by muscle contraction and involves a distinct subset of GLUT-4[66,151-153]. These pathways can involve nitric oxide[154] and activation of AMPK[155,156] as well as cytosolic calcium[130] but these effects are distinct and additive to those of insulin mediated glucose uptake[2,157-159]. Probably most important for T2D research is that these contraction mediated glucose pathways are not only present in T2D but are fully functional[160,161].
Interestingly, in insulin resistant muscle there seems to be a difference in the control of muscle protein synthesis. It appears that in tissue where the upstream activators of the mTORC1 pathway are impaired there are alterations to the use in protein syn
One key player that may have an impact on muscle protein synthesis in response to insulin is a serine/threonine kinase called PKC. PKC has long been considered as a regulatory contributor during mRNA translation in a number of tissues[162,163] but more recently specific isoforms of PKC have been implicated in the regulation of glucose uptake. Specifically, the conventional family of PKCs (α, β, γ) lead to atte
The regulation of PKC, like many of the enzymes related to insulin signal trans
Dysregulation of mTOR signaling is a key player in the development of many disease states including diabetes. While decades of research have been dedicated to under
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Specialty type: Biochemistry and molecular biology
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