CETN1

Last update 01 Nov 2024

Basic Info

Synonyms

Caltractin isoform 2, CEN1, centrin 1

+ [3]

Introduction

Plays a fundamental role in microtubule-organizing center structure and function (PubMed:8175926). Plays a role in sperm cilia formation (By similarity).

100 Clinical Results associated with CETN1

100 Translational Medicine associated with CETN1

0 Patents (Medical) associated with CETN1

Literatures (Medical) associated with CETN1

31 Dec 2024·Systems Biology in Reproductive Medicine

Identification of potential differences in salivary proteomic profiles between estrus and diestrus stage of estrous cycle in dairy cows

Article

Author: Manimaran, Ayyasamy ; Sinha, Manish Kumar ; Patil, Shivanagouda ; Nag, Pradeep ; Ramesha, Kerekoppa ; Kumaresan, Arumugam ; Jeyakumar, Sakthivel ; Shaji, Arsha ; Gowdar Veerappa, Vedamurthy

In the present study, a comparative global high-throughput proteomic analysis strategy was used to identify proteomic differences between estrus and diestrus stage of estrous cycle in dairy cows. Saliva was collected from cows during estrus and diestrus, and subjected to LC-MS/MS-based proteomic analysis. A total of 2842 proteins were detected in the saliva of cows, out of which, 2437 and 1428 non-redundant proteins were identified in estrous and diestrous saliva, respectively. Further, it was found that 1414 and 405 salivary proteins were specific to estrus and diestrus, respectively while 1023 proteins were common to both groups. Among the significantly dysregulated proteins, the expression of 56 proteins was down-regulated (abundance ratio <0.5) while 40 proteins were up-regulated (abundance ratio > 2) in estrous compared to diestrous saliva. The proteins, such as HSD17B12, INHBA, HSP70, ENO1, SRD5A1, MOS, AMH, ECE2, PDGFA, OPRK1, SYN1, CCNC, PLIN5, CETN1, AKR1C4, NMNAT1, CYP2E1, and CYP19A1 were detected only in the saliva samples derived from estrous cows. Considerable number of proteins detected in the saliva of estrous cows were found to be involved in metabolic pathway, PI3K-Akt signaling pathway, toll-like receptor signaling pathway, steroid biosynthesis pathway, insulin signaling pathway, calcium signaling pathway, estrogen signaling pathway, oxytocin signaling pathway, TGF-β signaling pathway and oocyte meiosis. On the other hand, proteins detected in saliva of diestrous cows were involved mainly in metabolic pathway. Collectively, these data provide preliminary evidence of a potential difference in salivary proteins at different stages of estrous cycle in dairy cows.

13 Sep 2024·ACS Infectious Diseases

Identifying Rab2 Protein as a Key Interactor of Centrin1 Essential for Leishmania donovani Growth

Article

Author: Roshanara ; Baig, Mirza Sarwar ; Tandon, Rati ; Nakhasi, Hira L. ; Puri, Niti ; Selvapandiyan, Angamuthu ; Das, Sanchita ; Srivastava, Rahul

Previously, we have demonstrated that deletion of a growth-regulating gene (LdCen1) in the Leishmania donovani parasite (LdCen1^-/-) attenuated the parasite's intracellular amastigote growth but not the growth of extracellular promastigotes. LdCen1^-/- parasites were found to be safe and efficacious against homologous and heterologous Leishmania species as a vaccine candidate in animal models. The reason for the differential growth of LdCen1^-/- between the two stages of the parasite needed investigation. Here, we report that LdCen1 interacts with a novel Ras-associated binding protein in L. donovani (LdRab2) to compensate for the growth of LdCen1^-/- promastigotes. LdRab2 was isolated by protein pull-down from the parasite lysate, followed by nano-LC-MS/MS identification. The RAB domain sequence and the functional binding partners of the LdRab2 protein were predicted via Search Tool for the Retrieval of Interacting Proteins (STRING) analysis. The closeness of the LdRab2 protein to other reported centrin-binding proteins with different functions in other organisms was analyzed via phylogenetic analysis. Furthermore, in vitro and in silico analyses revealed that LdRab2 also interacts with other L. donovani centrins 3-5. Since centrin is a calcium-binding protein, we further investigated calcium-based interactions and found that the binding of LdRab2 to LdCen1 and LdCen4 is calcium-independent, whereas the interactions with LdCen3 and LdCen5 are calcium-dependent. The colocalization of LdCen1 and LdRab2 at the cellular basal-body region by immunofluorescence supports their possible functional association. The elevated expression of the LdRab2 protein in the mutant promastigotes suggested a probable role in compensating for the promastigote growth of this mutant strain, probably in association with other parasite centrins.

01 Sep 2024·Current Biology

Dynamic shape-shifting of the single-celled eukaryotic predator Lacrymaria via unconventional cytoskeletal components

Article

Author: Gu, Siyu ; Kang, Dingbang ; Jiang, Chuanqi ; Huang, Kaiyao ; Wang, Guangying ; Liao, Zaitian ; Xiong, Jie ; Chai, Xiaocui ; Miao, Wei ; Zhang, Jing ; Zhou, Fang ; Xiao, Yuan ; Ge, Feng ; Pan, Tingting ; Zhang, Chengcai ; Warren, Alan ; Hu, Che ; Qin, Weiwei ; Chen, Kai ; Yang, Mingkun

Eukaryotic cells depend on dynamic changes in shape to fulfill a wide range of cellular functions, maintain essential biological processes, and regulate cellular behavior. The single-celled, predatory ciliate Lacrymaria exhibits extraordinary dynamic shape-shifting using a flexible "neck" that can stretch 7-8 times the length of its body to capture prey. The molecular mechanism behind this morphological change remains a mystery. We have observed that when in an active state, Lacrymaria repeatedly extends and contracts its neck to enable 360-degree space search and prey capture. This remarkable morphological change involves a unique actin-myosin system rather than the Ca²⁺-dependent system found in other contractile ciliates. Two cytoskeletons are identified in the cortex of the Lacrymaria cell, namely the myoneme cytoskeleton and the microtubule cytoskeleton. The myoneme cytoskeleton is composed of centrin-myosin proteins, exhibiting distinct patterns between the neck and body, with their boundary seemingly associated with the position of the macronucleus. A novel giant protein forming a ladder-like structure was discovered as a component of the microtubule cytoskeleton. Thick centrin-myosin fibers are situated very close to the right side of the ladders in the neck but are far away from such structures in the body. This arrangement enables the decoupling of the neck and body. Plasmodium-like unconventional actin has been discovered in Lacrymaria, and this may form highly dynamic short filaments that could attach to the giant protein and myosin, facilitating coordination between the two cytoskeletons in the neck. In summary, this fascinating organism employs unconventional cytoskeletal components to accomplish its extraordinary dynamic shape-shifting.

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CETN1

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