Abstract

TRIM36 is a member of the tripartite motif (TRIM) family of RING-containing proteins, also known as Haprin, which was first discovered for its abundance in testis and found to be implicated in the spermatozoa acrosome reaction. TRIM36 is a microtubule-associated E3 ubiquitin ligase that plays a role in cytoskeletal organization, and according to data gathered in different species, coordinates growth speed and stability, acting on the microtubules’ plus end, and impacting on cell cycle progression. TRIM36 is also crucial for early developmental processes, in Xenopus, where it is needed for dorso-ventral axis formation, but also in humans as bi-allelic mutations in the TRIM36 gene cause a form of severe neural tube closure defect, called anencephaly. Here, we review TRIM36-related mechanisms implicated in such composite physiological and pathological processes.

Highlights

  • The tripartite motif (TRIM) family represents the largest sub-family of RING domaincontaining proteins

  • In this model and similar to the other species analyzed to date, TRIM36 was detected in the acrosomal region of elongating and elongated spermatids following the initiation of adult spermiogenesis [44]

  • Trim36 role in maintaining proper organization of the egg microtubular array requires intact E3 ubiquitin ligase activity [20] and the same was observed for the acrosome reaction [16]

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Summary

Introduction

The tripartite motif (TRIM) family represents the largest sub-family of RING domaincontaining proteins. As ubiquitination regulates the stability and activity of many proteins, if not all, it is no surprise that this family is implicated in a variety of cellular processes, from transcription to apoptosis, from cell cycle regulation to signal transduction [5,6,7]. This involvement, often associated with spatial and temporal specific expression, implicates TRIM proteins in many physiological processes and pathological conditions. Tcoh-elofcaastliezra-gtiroonwwinigtheinndteirsmcaedlleiadte filthe ‘pamluesnetnsdw’ aansdintdheeesdloewxecrlugdroedwianngdetnhdeipsrreesfeenrrceedotfoTaRs ItMhe3‘6mwinaussaelnsod’o[b2s2e]r. vPeludsoenndmsi’totic detecstpioinndilne aXnednocpyutsokegingesticconmfiidrmboeddythmatic, ruoptuobnutlreims [3169-,d2e1p] l(eFtiiognu,reth2eAir,Bn)u. mMbiecrrowtuabsurlee-s are duceedssaenndtiathl epirrobteeihnapvoiolyr mchearosttihc.atInseardvdeiatisosnt,rutrcatcukrianlgeloefmmenictrsoitnubeuuklearpyluotsicencedlslsgarnodwwthhose was dnyonna-dmiricesctiisontiaglhitnlytrciomn3t6r-odlleepdleftoerdpergogpse,rwchyitcohskceolrerteallaotersgawniitzhatliaocnk. oMf cicorrotitcuablurloetsa-have tion.mTuhlitsipleledrtoolecsonwciltuhdine tthheatcterlilm, e3.g6.m, ciagphttuarectmtoemcoborradnien-abtoeupnldusoergnadngelrloews athndthruems doidffeelrm- ementiabllryanmeso,dourglaatninizgegthroewmthitostpiceesdpiannddlesftoarbciloirtyreoctf sloegcarel gvaetgioentaol facrrharyosmnoescoemsseasr,ycrfoosrsc-loinrtki-with cal rothtaetaiocntin[2c4y]t.oskeleton and adhesion hubs, define the position of the actomyosin contractile ring during cytokinesis, define cell shape and sense/transduce mechano-tension forces [22]

TRIM36 Function in Embryonic Development
TRIM36 Is Involved in Spermatogenesis
Involvement of TRIM36 in Cancer
TRIM36 Biochemical Roles
Conclusions and Future Perspectives
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