Regulation of Clathrin-Mediated Endocytosis

Mettlen, Marcel; Chen, Ping Hung; Srinivasan, Saipraveen; Danuser, Gaudenz; Schmid, Sandra L.

doi:10.1146/annurev-biochem-062917-012644

Cited by 473 publications

(525 citation statements)

References 154 publications

(260 reference statements)

Supporting

Mentioning

457

Contrasting

Unclassified

Order By: Relevance

“…The images, as shown in Figure A, clearly showed the coated ultrastructures in the 10 −11 M melatonin group and the control group. CME can be divided into four stages, namely initiation, stabilization, maturation, and membrane fission . The formation of clathrin‐coated pits and vesicles is required for the process of CME, and coated pits according to the different stages can be dissected into four kinds for quantification .…”

Section: Resultsmentioning

confidence: 99%

“…The occurrence of CME requires the formation of clathrin‐coated pits, which are assembled by the major coat proteins, including clathrin triskelia and AP2. In addition to this, endocytic accessory proteins are involved, and the large GTPase dynamin is recruited to regulate early stages of CME and to catalyze membrane fission . The clathrin triskelia comprises clathrin heavy chains and light chains, and AP2 is a heterotetramer made up of α, β2, μ2, and σ2 subunits .…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Melatonin promotes human oocyte maturation and early embryo development by enhancing clathrin‐mediated endocytosis

Liu

et al. 2019

Journal of Pineal Research

View full text Add to dashboard Cite

Embryo development potential and reproductive clinical outcomes are all deeply rooted in oocyte maturation. Melatonin has been reported to promote oocyte maturation as an antioxidant in nonprimate species. Its antioxidative functions also help reduce plasma membrane rigidity, which facilitates clathrin‐mediated endocytosis (CME). Whether melatonin has effects on human oocyte maturation by regulating CME is worthy of exploration. In this study, we found that the optimal melatonin concentration for human oocyte maturation was 10−11 M, and the maturation rate of this group was 71.9% (P = .03). The metaphase II (MII) stage oocytes obtained by in vitro maturation with 10−11 M melatonin had a significantly higher fertilization rate (81.4% vs 61.4%, respectively, P = .017) and blastocyst rate (32.2% vs 15.8%, respectively, P = .039) compared to controls. During maturation, antioxidative melatonin greatly enhanced CME and decreased intra‐oocyte cAMP level. The former was evidenced by the increasing numbers of coated pits and vesicles, and the upregulated expression of two major CME markers—clathrin and adaptor protein‐2 (AP2). CME inhibitor dynasore increased intra‐oocyte cAMP level and blocked oocyte maturation, and melatonin could partly rescue oocyte maturation and significantly elevate the expression of clathrin and AP2 in the presence of dynasore. Therefore, we conclude that melatonin could promote human oocyte maturation and early embryo development through enhancing CME.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Melatonin promotes human oocyte maturation and early embryo development by enhancing clathrin‐mediated endocytosis

Liu

et al. 2019

Journal of Pineal Research

View full text Add to dashboard Cite

show abstract

“…Once the coated vesicle forms, it is released into the cytosol where it is uncoated and trafficked to an acceptor membrane for fusion and cargo delivery. Most transport vesicles in the periphery of the cell, including those originating from the plasma membrane, utilize a coat containing the three‐legged triskelion scaffold protein called clathrin (Figure A) …”

Section: Introductionmentioning

confidence: 99%

Conformational regulation of AP1 and AP2 clathrin adaptor complexes

Beacham

Partlow

Hollopeter

2019

Traffic

View full text Add to dashboard Cite

Heterotetrameric clathrin adaptor protein complexes (APs) orchestrate the formation of coated vesicles for transport among organelles of the cell periphery. AP1 binds membranes enriched for phosphatidylinositol 4‐phosphate, such as the trans Golgi network, while AP2 associates with phosphatidylinositol 4,5‐bisphosphate of the plasma membrane. At their respective membranes, AP1 and AP2 bind the cytoplasmic tails of transmembrane protein cargo and clathrin triskelions, thereby coupling cargo recruitment to coat polymerization. Structural, biochemical and genetic studies have revealed that APs undergo conformational rearrangements and reversible phosphorylation to cycle between different activity states. While membrane, cargo and clathrin have been demonstrated to promote AP activation, growing evidence supports that membrane‐associated proteins such as Arf1 and FCHo also stimulate this transition. APs may be returned to the inactive state via a regulated process involving phosphorylation and a protein called NECAP. Finally, because antiviral mechanisms often rely on appropriate trafficking of membrane proteins, viruses have evolved novel strategies to evade host defenses by influencing the conformation of APs. This review will cover recent advances in our understanding of the molecular inputs that stimulate AP1 and AP2 to adopt structurally and functionally distinct configurations.

show abstract

“…Starting at the plasma membrane, the internalization of intrinsic membrane proteins can occur by several endocytic pathways. Clathrin‐mediated endocytosis is the principal mechanism of internalization of receptor‐bound macromolecules, transporters and other membrane proteins (termed cargo) from the cell surface, and additional internalization mechanisms diversify the routes of cellular entry available to certain receptors, as reviewed in References . Vesicles derived from these processes are mainly delivered to early endosomes, which are membrane compartments that harbor early endosome antigen 1 (EEA1) and Rab5.…”

Section: Introductionmentioning

confidence: 99%

Energetic adaptations: Metabolic control of endocytic membrane traffic

Rahmani

Defferrari

Wakarchuk

et al. 2019

Traffic

View full text Add to dashboard Cite

Endocytic membrane traffic controls the access of myriad cell surface proteins to the extracellular milieu, and thus gates nutrient uptake, ion homeostasis, signaling, adhesion and migration. Coordination of the regulation of endocytic membrane traffic with a cell's metabolic needs represents an important facet of maintenance of homeostasis under variable conditions of nutrient availability and metabolic demand. Many studies have revealed intimate regulation of endocytic membrane traffic by metabolic cues, from the specific control of certain receptors or transporters, to broader adaptation or remodeling of the endocytic membrane network. We examine how metabolic sensors such as AMP‐activated protein kinase, mechanistic target of rapamycin complex 1 and hypoxia inducible factor 1 determine sufficiency of various metabolites, and in turn modulate cellular functions that includes control of endocytic membrane traffic. We also examine how certain metabolites can directly control endocytic traffic proteins, such as the regulation of specific protein glycosylation by limiting levels of uridine diphosphate N‐acetylglucosamine (UDP‐GlcNAc) produced by the hexosamine biosynthetic pathway. From these ideas emerge a growing appreciation that endocytic membrane traffic is orchestrated by many intrinsic signals derived from cell metabolism, allowing alignment of the functions of cell surface proteins with cellular metabolic requirements. Endocytic membrane traffic determines how cells interact with their environment, thus defining many aspects of nutrient uptake and energy consumption. We examine how intrinsic signals that reflect metabolic status of a cell regulate endocytic traffic of specific proteins, and, in some cases, exert broad control of endocytic membrane traffic phenomena. Hence, endocytic traffic is versatile and adaptable and can be modulated to meet the changing metabolic requirements of a cell.

show abstract

Regulation of Clathrin-Mediated Endocytosis

Cited by 473 publications

References 154 publications

Melatonin promotes human oocyte maturation and early embryo development by enhancing clathrin‐mediated endocytosis

Melatonin promotes human oocyte maturation and early embryo development by enhancing clathrin‐mediated endocytosis

Conformational regulation of AP1 and AP2 clathrin adaptor complexes

Energetic adaptations: Metabolic control of endocytic membrane traffic

Contact Info

Product

Resources

About