Dynamin and the Actin Cytoskeleton Cooperatively Regulate Plasma Membrane Invagination by BAR and F-BAR Proteins

Itoh, Toshiki; Erdmann, Kai S.; Roux, Aurélien; Habermann, Bianca; Werner, Hauke; Camilli, Pietro De

doi:10.1016/j.devcel.2005.11.005

Cited by 549 publications

(734 citation statements)

References 78 publications

Supporting

Mentioning

690

Contrasting

Unclassified

Order By: Relevance

“…In fungi, this actin activity of the myosins could supplant the requirement of a dynamin-like protein in neck elongation/ vesicle scission, and simultaneously provide an actin component to the process as well. Consistent with this idea, it has been suggested recently that a role for dynamin in animal cells is to help create elongated tubules, whereas tension mediated by the actin cytoskeleton is required for the scission of these tubules (Itoh et al, 2005). Additionally, a recent report shows that Myosin IE interacts with dynamin and the 5Ј inositol phosphatase synaptojanin, further suggesting a physical and potential regulatory link between type I myosins and scission machinery (Krendel et al, 2007).…”

Section: Discussionmentioning

confidence: 70%

Interaction of the Endocytic Scaffold Protein Pan1 with the Type I Myosins Contributes to the Late Stages of Endocytosis

Barker

Lee

Pierce

et al. 2007

MBoC

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 70%

Interaction of the Endocytic Scaffold Protein Pan1 with the Type I Myosins Contributes to the Late Stages of Endocytosis

Barker

Lee

Pierce

et al. 2007

MBoC

View full text Add to dashboard Cite

“…CIP4/2 (Cdc42-interacting protein 4/2) is a modular domain protein containing an FCH domain, which has been recently recognized as part of a larger structural domain called EFC or F-BAR. This domain is similar to the BAR domain that is involved in regulating membrane curvature [88,89]. In addition, CIP4/2 also contain two coiled-coil domains, and an SH3 domain that is recruited to the plasma membrane in response to insulin activation of TC10.…”

Section: Insulin Signaling Leading To Glut4 Translocationmentioning

confidence: 99%

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Hou

Pessin

2007

Current Opinion in Cell Biology

130

116

View full text Add to dashboard Cite

SummaryGlucose transporter 4 (GLUT4) is the major insulin regulated glucose transporter expressed mainly in muscle and adipose tissue. GLUT4 is stored in a poorly characterized intracellular vesicular compartment and translocates to the cell surface in response to insulin stimulation resulting in increase glucose uptake. This process is essential for the maintenance of normal glucose homeostasis and involves a complex interplay of trafficking events and intracellular signaling cascades. Recent studies have identified sortilin as an essential element for the formation of GLUT4 storage vesicles during adipogenesis and GGA (Golgi-localized γ-ear-containing Arf-binding protein) as a key coat adaptor for the entry of newly synthesized GLUT4 into the specialized compartment. Insulinstimulated GLUT4 translocation from this compartment to the plasma membrane appears to require the Akt/protein kinase B substrate, termed AS160 (Akt Substrate of 160 kDa). In addition, the VPS9 domain-containing protein Gapex-5 in complex with CIP4 appears to function as a Rab31 guanylnucleotide exchange factor that is necessary for insulin-stimulated GLUT4 translocation. Here we attempt to summaries recent advances in GLUT4 vesicle biogenesis, intracellular trafficking and membrane fusion.

show abstract

“…2A). N-terminal myc tagged constructs were generated for wild-type PACSIN3 (WT), a C-terminal truncation which deleted the SH3 domain (ΔC354), a C-terminal truncation that deleted the proline rich domain (PXXP) as well as the SH3 domain (ΔC329), and an Nterminal deletion construct that removed the polybasic region (also called the F-BAR domain [16]) (ΔN244). Upon infection of adipocytes, each construct was expressed and migrated on SDS gels at its predicted molecular weight (data not shown).…”

Section: Pacsin3 Overexpression Elevates Glucose Uptakementioning

confidence: 99%

PACSIN3 overexpression increases adipocyte glucose transport through GLUT1

Roach¹,

Plomann²

2007

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

PACSIN family members regulate intracellular vesicle trafficking via their ability to regulate cytoskeletal rearrangement. These processes are known to be involved in trafficking of GLUT1 and GLUT4 in adipocytes. In this study PACSIN3 was observed to be the only PACSIN isoform that increases in expression during 3T3-L1 adipocyte differentiation. Overexpression of PACSIN3 in 3T3-L1 adipocytes caused an elevation of glucose uptake. Subcellular fractionation revealed that PACSIN3 overexpression elevated GLUT1 plasma membrane localization without effecting GLUT4 distribution. In agreement with this result, examination of GLUT exofacial presentation at the cell surface by photoaffinity labeling revealed significantly increased GLUT1, but not GLUT4, after overexpression of PACSIN3. These results establish a role for PACSIN3 in regulating glucose uptake in adipocytes via its preferential participation in GLUT1 trafficking. They are consistent with the proposal, which is supported by a recent study, that GLUT1, but not GLUT4, is predominantly endocytosed via the coated pit pathway in unstimulated 3T3-L1 adipocytes. Keywordsadipocyte; endocytosis; GLUT1; GLUT4; PACSIN3; membrane trafficking; syndapin The need to transport glucose from outside to inside the cell is a fundamental feature of cellular survival and growth. In mammals glucose transport of the facilitated diffusion type is mediated by a group of transporters known as the GLUT family (SLC2A gene symbol). The GLUT's comprise a 13-member family of 12-trans-membrane spanning 50-60 kD proteins [1]. Among these, GLUT1 and GLUT4 are of central relevance to peripheral glucose disposal and have been extensively studied. Nevertheless, the mechanisms involved in controlling the trafficking of GLUT1 and GLUT4 to and from the plasma membrane, and the differences between the trafficking of the two GLUT's, are not completely understood [2,3]. It is possible that proteins involved in integrating cytoskeletal rearrangements with membrane trafficking participate in these mechanisms. Recent studies have identified adaptor proteins that do coordinate membrane trafficking events with alterations in the cytoskeleton. Major examples are the amphiphysin, cortactin, endophilin, intersectin and syndapin/PACSIN families [4][5][6][7]. These proteins contain multiple protein-protein interaction domains, which allow them to *Address correspondence to William Roach at present address: Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755-3844. william.roach@dartmouth.edu. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. In thi...

show abstract

Dynamin and the Actin Cytoskeleton Cooperatively Regulate Plasma Membrane Invagination by BAR and F-BAR Proteins

Cited by 549 publications

References 78 publications

Interaction of the Endocytic Scaffold Protein Pan1 with the Type I Myosins Contributes to the Late Stages of Endocytosis

Interaction of the Endocytic Scaffold Protein Pan1 with the Type I Myosins Contributes to the Late Stages of Endocytosis

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

PACSIN3 overexpression increases adipocyte glucose transport through GLUT1

Contact Info

Product

Resources

About