Clathrin

Kirchhausen, Tomas

doi:10.1146/annurev.biochem.69.1.699

Cited by 562 publications

(542 citation statements)

References 149 publications

(156 reference statements)

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“…The background scattering intensity from the cuvette and solvent was less than 1% of the detected signal in all experiments. In the Guinier regime (qR g ≪ 1), the angular dependence of the scattered intensity, I(q), is well-approximated by a Gaussian profile with a width related to the R g (1) where the scalar quantity q is the magnitude of the Bragg scattering wave vector (9), viz. (2) with λ, θ, and n being the wavelength, the scattering angle, and the refractive index of the solution, respectively.…”

Section: Slsmentioning

confidence: 99%

Conformation of a Clathrin Triskelion in Solution

et al. 2006

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A principal component in the protein coats of certain post-golgi and endocytic vesicles is clathrin, which appears as a three-legged heteropolymer (known as a triskelion) that assembles into polyhedral cages principally made up of pentagonal and hexagonal faces. In vitro, this assembly depends upon the pH, with cages forming more readily at low pH and less readily at high pH. We have developed procedures, on the basis of static and dynamic light scattering, to determine the radius of gyration, R g , and hydrodynamic radius, R H , of isolated triskelia, under conditions where cage assembly occurs. Calculations based on rigid molecular bead models of a triskelion show that the measured values can be accounted for by bending the legs and a puckering at the vertex. We also show that the values of R g and R H measured for clathrin triskelia in solution are qualitatively consistent with the conformation of a triskelion in a "D 6 barrel" cage assembly measured by cryoelectron microscopy.A major component of the protein coats of certain endocytic vesicles is clathrin, a heteropolymer composed of a 192 kDa heavy chain and a variable, ca. 23-27 kDa, associated light chain (1). Three clathrin molecules join at a common hub to form a threelegged "triskelion", which is the basic building block of the coats. Each leg is approximately 3.0 nm thick and 52.0 nm in length and ends in a globular "terminal domain" of radius 5.0 nm. By convention, a leg is divided into a proximal segment adjoining the central hub, a linker region, and a distal segment that connects with the terminal domain. A clathrin heavy chain runs the entire length of the leg, with a light chain attached near the common hub (see Figure 1). In vitro, the triskelia assemble into polyhedral cages (or "baskets") composed of pentagonal and hexagonal faces (2), mimicking the structures seen on the outside of endocytic vesicles. One can dissociate baskets or uncoat vesicles by changing the properties † This work was supported by extramural grants from the National Institutes of Health and intramural funds from the National Institute HHS Public Access Author Manuscript Author ManuscriptAuthor ManuscriptAuthor Manuscript of the solution in which they are suspended (e.g., by changing pH and ionic strength) (3) or by adding an uncoating ATPase (4).Triskelia assemble at low pH to form baskets (3) or at higher pH, when clathrin assembly proteins (e.g., AP-2, AP-180, etc.) are added (5). It is not currently known why these conditions favor assembly. Possible mechanisms supporting assembly at low pH include conformational changes in the tertiary structure of the triskelia, which might relieve steric hindrances to basket assembly, and enhanced interactions between the intertwined triskelia that form the basket struts. The role of APs as assembly proteins may be to increase mechanical linkages between the triskelia (5-7).In this paper, we report light-scattering measurements on clathrin in solution, including conditions where assembly occurs. From static light scatteri...

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Section: Slsmentioning

confidence: 99%

Conformation of a Clathrin Triskelion in Solution

et al. 2006

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“…In the clathrin-mediated endocytic pathway, clathrin is composed of a trimer of CHC and is associated with each light chain, called triskelion, and they further assemble to form a polyhedral cage-like structure (Kirchhausen, 2000). Polyhedral clathrin is recruited to the plasma membrane and promotes the internalization of certain receptors to take nutrients or to transduce correct intracellular signaling from receptors (McPherson et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription

et al. 2007

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“…The inhibitory activity of each peak from either the soluble or sedimentable fraction was similar to that of CLb purified from the post-MT supernatant despite the presence of a 37-kDa protein most likely to be CLa [9,13]: 60-90% inhibition of MT-PP1 activity was produced by the CLb at the concentration where it was marginally detected by immunoblotting under the conditions (Fig. 3, arbitrary concentration 16 in B, 8 in C and D; 2.4 nM in E).…”

Section: Clb Purified From Post-mt Supernatant Potently Inhibitsmentioning

confidence: 80%

“…1) and incorrectly large molecular masses indicated by electrophoretic mobilities in SDS-PAGE ( [9] and estimation for brain CLb of 25.1 kDa [12] to be 29 and 32 kDa in Fig. 1).…”

Section: Clb Purified From Post-mt Supernatant Potently Inhibitsmentioning

confidence: 88%

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Clathrin light chain b is capable of affecting potently a major protein phosphatase from microtubules (MT‐PP1)

Hiraga¹,

Morrice²,

Honda³

et al. 2006

FEBS Letters

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Clathrin light chain (CL) b purified from bovine brain postmicrotubule supernatant and identified by mass spectrometry potently inhibited a catalytic activity of a major protein phosphatase (PP) that was copurified with microtubules and recognized by antiPP1 antibodies. CLb similarly affected the catalytic subunit and holoenzyme of the PP, little inhibiting the activity of PP2A. Although the CLb from clathrin-coated vesicles was several hundredfold weaker than our purified CLb, the CLb in the postmicrotubule supernatant, independent of whether it was sedimentable or soluble, was as active as the purified CLb. Thus CLb may be a potent regulator of the PP.

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Clathrin

Cited by 562 publications

References 149 publications

Conformation of a Clathrin Triskelion in Solution

Conformation of a Clathrin Triskelion in Solution

Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription

Clathrin light chain b is capable of affecting potently a major protein phosphatase from microtubules (MT‐PP1)

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