Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase

Sulpizio, Alan; Minelli, Marena E.; Mao, Yuxin

doi:10.1016/j.tim.2019.09.001

Cited by 12 publications

(12 citation statements)

References 8 publications

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“…Compartmentalization of SidJ's activity in the host cytosol prevents premature inactivation of SidE effectors before being injected into the host cell. Biochemical studies have revealed that the association of SidJ with CaM stabilizes the active conformation of the effector ( 138 , 139 , 140 , 141 , 142 ). Structure–function studies ( 138 , 139 , 140 , 141 ) revealed SidJ to be a pseudokinase that utilizes ATP to catalyze the polyglutamylation of SdeA (and other SidE members).…”

Section: Side Proteins Sidj and Sded: Atypical Ubiquitination Of Rab-gtpasesmentioning

confidence: 99%

The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis

Iyer

Das

2021

Journal of Biological Chemistry

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Section: Side Proteins Sidj and Sded: Atypical Ubiquitination Of Rab-gtpasesmentioning

confidence: 99%

The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis

Iyer

Das

2021

Journal of Biological Chemistry

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“…Several other examples of such L. pneumophila effector cascades exist, including SidE family effectors that catalyze phosphoribosylation of ubiquitin (PR‐Ub) to promote serine ubiquitination on host proteins (Sulpizio et al , ). The activity of SidEs is counteracted by two PDE domain‐containing effectors, DupA and DupB, that function as deubiquitinases to specifically cleave PR‐Ub from PR‐ubiquitinated substrates and reverse the E1‐ and E2‐independent ubiquitination by SidEs (Fig ).…”

Section: E1‐ and E2‐independent Ubiquitination And Regulation By Legimentioning

confidence: 99%

“…The activity of SidEs is counteracted by two PDE domain‐containing effectors, DupA and DupB, that function as deubiquitinases to specifically cleave PR‐Ub from PR‐ubiquitinated substrates and reverse the E1‐ and E2‐independent ubiquitination by SidEs (Fig ). Moreover, the ubiquitin ligase activity of SidEs is inhibited by SidJ via calmodulin‐mediated glutamylation (Sulpizio et al , ) (Fig ). Similar successive regulation of host target including modification, reversal, and inhibition by Legionella effectors also occurs on the host small GTPase Rab1, which is sequentially modulated by SidM, LepB, SidD, AnkX, and Lem3 (Goody & Itzen, ).…”

Section: E1‐ and E2‐independent Ubiquitination And Regulation By Legimentioning

confidence: 99%

Legionella pneumophila balances ubiquitin transglutamination

2020

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The effector MavC of the bacterial pathogen Legionella pneumophila catalyzes a noncanonical ubiquitination of the host ubiquitin‐conjugating E2 enzyme UBE2N by crosslinking a glutamine residue of ubiquitin to UBE2N lysine residues via its transglutaminase activity. A new study by Gan et al (2020) reveals that L. pneumophila reverses this noncanonical ubiquitination via its ubiquitin deamidase effector MvcA to allow precise temporal regulation of host signaling during infection.

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“…25 The Sde family of L. pneumophila proteins is a set of four proteins translocated by the T4SS that are required for optimal growth in amoebae, 26 with biochemical activities subject to extensive regulation by at least three other effectors. [27][28][29][30][31][32] Each Sde protein has three domains, shown by either sequence similarity or biochemical analysis to control ubiquitin (Ub) dynamics (Fig. 1A and B).…”

Section: Introductionmentioning

confidence: 99%