Investigations on Cellular Localization of Coiled-Coil Domain-Containing Protein 43  (CCDC43) Under Stress Conditions

Merve Tuzlakoğlu Öztürk

Makale detayları

Investigations on Cellular Localization of Coiled-Coil Domain-Containing Protein 43 (CCDC43) Under Stress Conditions

Yazarlar:

Merve Tuzlakoğlu Öztürk

Yayıncı:

Manisa Celal Bayar University

Ana Başlıklar:

Bitki Hücresi ve Moleküler Biyoloji

Dergi:

Celal Bayar Üniversitesi Fen Bilimleri Dergisi Vol.21 Issue 3, pp.21-27

Belge Tipi:

Makale

Yayın Tarihi:

9/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001359115

pISSN:

1305-130X

Anahtar kelimeler:

Özet:

 Coiled-coil domain containing CCDC family proteins regulate multiple biological functions in the cell. These domain structures have physical properties favorable for liquid-liquid phase separation LLPS phenomena, which play important roles in cell biology dynamics. LLPS is a fundamental mechanism in forming membrane-less organelles, including stress granules SG and P-body, nucleolus, PML nuclear body, Cajal bodies, nuclear speckles, and centrosomes. One of the new members of the CCDC protein family is CCDC43. In this study, sequence-based analyses of CCDC43, performed as a first step to understanding the role of CCDC43 in the cellular network, revealed the LLPS potential of the protein. We report that CCDC43, which has an evolutionarily conserved protein sequence, structurally possesses RNA-binding sites and its amino acid composition analysis may show an aggregation propensity and LLPS behavior under cellular conditions. CCDC43 is known to show a diffuse localization in the cytoplasm. We investigated whether this cellular localization is present in SGs whose formation is based on LLPS. We found that CCDC43 does not aggregate at SGs under given stress conditions. These data provide the first insights into the intracellular behavior and roles of CCDC43 in a disease-independent manner.

 Coiled-coil domain containing CCDC family proteins regulate multiple biological functions in the cell. These domain structures have physical properties favorable for liquid-liquid phase separation LLPS phenomena, which play important roles in cell biology dynamics. LLPS is a fundamental mechanism in forming membrane-less organelles, including stress granules SG and P-body, nucleolus, PML nuclear body, Cajal bodies, nuclear speckles, and centrosomes. One of the new members of the CCDC protein family is CCDC43. In this study, sequence-based analyses of CCDC43, performed as a first step to understanding the role of CCDC43 in the cellular network, revealed the LLPS potential of the protein. We report that CCDC43, which has an evolutionarily conserved protein sequence, structurally possesses RNA-binding sites and its amino acid composition analysis may show an aggregation propensity and LLPS behavior under cellular conditions. CCDC43 is known to show a diffuse localization in the cytoplasm. We investigated whether this cellular localization is present in SGs whose formation is based on LLPS. We found that CCDC43 does not aggregate at SGs under given stress conditions. These data provide the first insights into the intracellular behavior and roles of CCDC43 in a disease-independent manner.

 Coiled-coil domain containing CCDC family proteins regulate multiple biological functions in the cell. These domain structures have physical properties favorable for liquid-liquid phase separation LLPS phenomena, which play important roles in cell biology dynamics. LLPS is a fundamental mechanism in forming membrane-less organelles, including stress granules SG and P-body, nucleolus, PML nuclear body, Cajal bodies, nuclear speckles, and centrosomes. One of the new members of the CCDC protein family is CCDC43. In this study, sequence-based analyses of CCDC43, performed as a first step to understanding the role of CCDC43 in the cellular network, revealed the LLPS potential of the protein. We report that CCDC43, which has an evolutionarily conserved protein sequence, structurally possesses RNA-binding sites and its amino acid composition analysis may show an aggregation propensity and LLPS behavior under cellular conditions. CCDC43 is known to show a diffuse localization in the cytoplasm. We investigated whether this cellular localization is present in SGs whose formation is based on LLPS. We found that CCDC43 does not aggregate at SGs under given stress conditions. These data provide the first insights into the intracellular behavior and roles of CCDC43 in a disease-independent manner.

 ÖZET Sarılı-sarmal domain ailesi proteinleri hücrede çoklu biyolojik fonksiyonları düzenler. Bu domain yapıları, hücre biyolojisi dinamiklerinde önemli roller oynayan sıvı-sıvı faz ayrımı LLPS olayları için uygun fiziksel özelliklere sahiptir. LLPS, stres granülleri SG ve P-cisimciği, nükleolus, PML nükleer cisimciği, Cajal cisimcikleri, nükleer benekler ve sentrozomlar dahil olmak üzere zarsız organellerin oluşturulmasında temel bir mekanizmadır. CCDC protein ailesinin daha az çalışılmış üyelerinden biri CCDC43tür. Bu çalışmada, CCDC43ün hücresel ağdaki rolünü anlamak için ilk adım olarak gerçekleştirilen CCDC43ün sekans bazlı analizleri, proteinin LLPS potansiyelini ortaya koymuştur. Evrimsel olarak korunmuş bir protein dizisine sahip olan CCDC43ün yapısal olarak RNA bağlanma bölgelerine sahip olduğunu ve amino asit kompozisyon analizinin hücresel koşullar altında bir agregasyon eğilimi ve LLPS davranışı gösterebileceğini bildiriyoruz. CCDC43ün sitoplazmada yaygın bir lokalizasyon gösterdiği bilinmektedir. Bu hücresel lokalizasyonun, oluşumu LLPSye dayanan SGlerde mevcut olup olmadığını araştırdık. CCDC43ün verilen stres koşulları altında SGlerde toplanmadığını bulduk. Bu veriler, hastalıktan bağımsız bir şekilde CCDC43ün hücre içi davranışı ve rolleri hakkında ilk bilgileri sağlamaktadır.

Makale detayları

Investigations on Cellular Localization of Coiled-Coil Domain-Containing Protein 43 (CCDC43) Under Stress Conditions

Yazarlar:

Merve Tuzlakoğlu Öztürk

Yayıncı:

Manisa Celal Bayar University

Ana Başlıklar:

Bitki Hücresi ve Moleküler Biyoloji

Dergi:

Celal Bayar Üniversitesi Fen Bilimleri Dergisi Vol.21 Issue 3, pp.21-27

Belge Tipi:

Makale

Yayın Tarihi:

9/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001359115

pISSN:

1305-130X

CCDC43

liquid-liquid phase separation

stress granulesCCDC43

sıvı-sıvı faz ayrımı

stres granül

Sayı

Makale detayları

Investigations on Cellular Localization of Coiled-Coil Domain-Containing Protein 43 (CCDC43) Under Stress Conditions

Yazarlar: Merve Tuzlakoğlu Öztürk

Yayıncı: Manisa Celal Bayar University

Ana Başlıklar: Bitki Hücresi ve Moleküler Biyoloji

Dergi: Celal Bayar Üniversitesi Fen Bilimleri Dergisi Vol.21 Issue 3, pp.21-27

Belge Tipi: Makale

Yayın Tarihi: 9/2025

Belge Dili: İngilizce

Document ID (Org No.): 2001359115

pISSN: 1305-130X

CCDC43

liquid-liquid phase separation

stress granulesCCDC43

sıvı-sıvı faz ayrımı

stres granül

Sayı

Yazarlar:

Merve Tuzlakoğlu Öztürk

Yayıncı:

Manisa Celal Bayar University

Ana Başlıklar:

Bitki Hücresi ve Moleküler Biyoloji

Dergi:

Celal Bayar Üniversitesi Fen Bilimleri Dergisi Vol.21 Issue 3, pp.21-27

Belge Tipi:

Makale

Yayın Tarihi:

9/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001359115

pISSN:

1305-130X